Structure of PDB 6ciq Chain C

Receptor sequence

>6ciqC (length=1161) Species: 264732 (Moorella thermoacetica ATCC 39073)

PKQTLDGNTAAAHVAYAMSEVATIYPITPSSPMAEIADEWAAHGRKNIFG
KTLQVAEMQSEAGAAGAVHGSLAAGALTTTFTASQGLLLMIPNMYKIAGE
LLPCVFHVAARALSTHALSIFGDHADVMAARQTGFAMLSSASVQEVMDLA
LVAHLATLKARVPFVHFFDGFRTSHEVQKIDVIEYEDMAKLVDWDAIRAF
RQRALNPEHPHQRGTAQNPDIYFQSREAANPYYLATPGIVAQVMEQVAGL
TGRHYHLFDYAGAPDAERVIVSMGSSCEVIEETVNYLVEKGEKVGLIKVR
LFRPFSAEHFLKVLPASVKRIAVLDRTKEPGSLGEPLYEDVQTVLAEHGK
NILVVGGRYGLGSKEFNPSMVKAVFDNLAATTPKNKFTVGITDDVTHTSL
EIKEHIDTSPKGTFRCKFFGLGSDGTVGANKNSIKIIGDHTDMYAQGYFV
YDSKKSGGVTISHLRFGKQPIQSAYLIDQADLIACHNPSYVGRYNLLEGI
KPGGIFLLNSTWSAEEMDSRLPADMKRTIATKKLKFYNIDAVKIAQEIGL
GSRINVIMQTAFFKIANVIPVDEAIKYIKDSIVKTYGKKGDKILNMNFAA
VDRALEALEEIKYPASWADAVEEPEFIQKVLRPINALKGDELPVSTFTPD
GVFPVGTTKYEKRGIAVNIPQWQPENCIQCNQCSLVCPHAAIRPYLAKPA
DLAGAPETFVTKDAIGKEAAGLKFRIQVSPLDCTGCGNCADVCPAKVKAL
TMVPLEEVTAVEEANYNFAEQLPEVKVNFNPATVKGSQFRQPLLEFSGAC
AGCGETPYVKLVTQLFGDRMIIANATGCSSIWGGSAPACPYTVNRQGHGP
AWASSLFEDNAEFGYGMALAVAKRQDELATAISKALEAPVSAAFKAACEG
WLAGKDDADRSREYGDRIKALLPGEISQASGEVKDLLLDIDRQKDYLTKK
SIWIIGGDGWAYDIGYGGLDHVLASGANVNVLVLDTEVYSNTGGQSSKAT
QTGAVARFAAGGKFTKKKDLGLMAMSYGYVYVASVAMGASHSQLMKALIE
AEKYDGPSLIIAYAPCINHGINMTYSQREAKKAVEAGYWPLYRYNPQLAQ
EGKNPFILDYKTPTASFRDFLMGEIRYTSLKKQFPEKAEQLFAKAEADAK
ARLEQYKKLAE

3D structure

• PDB: 6ciq Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase fromMoorella thermoacetica.
• Chain: C
• Resolution: 3.302 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T29 E62 R112 N1000
• Catalytic site (residue number reindexed from 1): T28 E61 R111 N991
• Enzyme Commision number: 1.2.7.1: pyruvate synthase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	SF4	C	W681 C686 I687 C689 N690 C692 C752 A758	W672 C677 I678 C680 N681 C683 C743 A749
BS02	SF4	C	P679 C696 P697 I701 C742 T743 G744 C745 G746 C748	P670 C687 P688 I692 C733 T734 G735 C736 G737 C739
BS03	SF4	C	A808 C809 C812 E814 C837 S999 C1075 I1076	A799 C800 C803 E805 C828 S990 C1066 I1067
BS04	TPP	C	P27 I28 E62 Q86 E814 G836 C837 F866 G966 D967 G968 V997 Y998 S999 N1000 T1001	P26 I27 E61 Q85 E805 G827 C828 F857 G957 D958 G959 V988 Y989 S990 N991 T992
BS05	MG	C	D967 T995 V997	D958 T986 V988
BS06	COA	C	T29 I121 S424 G426 V428 Y452 K456 R554 N556 Y587 N598 N1000 T1001	T28 I120 S423 G425 V427 Y451 K455 R553 N555 Y586 N597 N991 T992

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0005506 iron ion binding
• GO:0016491 oxidoreductase activity
• GO:0016903 oxidoreductase activity, acting on the aldehyde or oxo group of donors
• GO:0019164 pyruvate synthase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0046872 metal ion binding
• GO:0051539 4 iron, 4 sulfur cluster binding

Biological Process

• GO:0006086 acetyl-CoA biosynthetic process from pyruvate
• GO:0006979 response to oxidative stress
• GO:0022900 electron transport chain

External links

• PDB: RCSB:6ciq, PDBe:6ciq, PDBj:6ciq
• PDBsum: 6ciq
• PubMed: 29581263
• UniProt: Q2RMD6|PFOR_MOOTA Pyruvate:ferredoxin oxidoreductase (Gene Name=Moth_0064)