Structure of PDB 6ciq Chain A

Receptor sequence

>6ciqA (length=1169) Species: 264732 (Moorella thermoacetica ATCC 39073)

PKQTLDGNTAAAHVAYAMSEVATIYPITPSSPMAEIADEWAAHGRKNIFG
KTLQVAEMQSEAGAAGAVHGSLAAGALTTTFTASQGLLLMIPNMYKIAGE
LLPCVFHVAARALSTHALSIFGDHADVMAARQTGFAMLSSASVQEVMDLA
LVAHLATLKARVPFVHFFDGFRTSHEVQKIDVIEYEDMAKLVDWDAIRAF
RQRALNPEHPHQRGTAQNPDIYFQSREAANPYYLATPGIVAQVMEQVAGL
TGRHYHLFDYAGAPDAERVIVSMGSSCEVIEETVNYLVEKGEKVGLIKVR
LFRPFSAEHFLKVLPASVKRIAVLDRTKEPGSLGEPLYEDVQTVLAEHGK
NILVVGGRYGLGSKEFNPSMVKAVFDNLAATTPKNKFTVGITDDVTHTSL
EIKEHIDTSPKGTFRCKFFGLGSDGTVGANKNSIKIIGDHTDMYAQGYFV
YDSKKSGGVTISHLRFGKQPIQSAYLIDQADLIACHNPSYVGRYNLLEGI
KPGGIFLLNSTWSAEEMDSRLPADMKRTIATKKLKFYNIDAVKIAQEIGL
GSRINVIMQTAFFKIANVIPVDEAIKYIKDSIVKTYGKKGDKILNMNFAA
VDRALEALEEIKYPASWADAVDEAAATVTEEPEFIQKVLRPINALKGDEL
PVSTFTPDGVFPVGTTKYEKRGIAVNIPQWQPENCIQCNQCSLVCPHAAI
RPYLAKPADLAGAPETFVTKDAIGKEAAGLKFRIQVSPLDCTGCGNCADV
CPAKVKALTMVPLEEVTAVEEANYNFAEQLPEVKVNFNPATVKGSQFRQP
LLEFSGACAGCGETPYVKLVTQLFGDRMIIANATGCSSIWGGSAPACPYT
VNRQGHGPAWASSLFEDNAEFGYGMALAVAKRQDELATAISKALEAPVSA
AFKAACEGWLAGKDDADRSREYGDRIKALLPGEISQASGEVKDLLLDIDR
QKDYLTKKSIWIIGGDGWAYDIGYGGLDHVLASGANVNVLVLDTEVYSNT
GGQSSKATQTGAVARFAAGGKFTKKKDLGLMAMSYGYVYVASVAMGASHS
QLMKALIEAEKYDGPSLIIAYAPCINHGINMTYSQREAKKAVEAGYWPLY
RYNPQLAQEGKNPFILDYKTPTASFRDFLMGEIRYTSLKKQFPEKAEQLF
AKAEADAKARLEQYKKLAE

3D structure

• PDB: 6ciq Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase fromMoorella thermoacetica.
• Chain: A
• 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 N999
• 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	A	W681 C686 I687 C689 N690 C692 I735 C752 A758	W680 C685 I686 C688 N689 C691 I734 C751 A757
BS02	SF4	A	P679 C696 P697 I701 C742 T743 G744 C745 G746 C748	P678 C695 P696 I700 C741 T742 G743 C744 G745 C747
BS03	SF4	A	A808 C809 C812 E814 C837 S999 C1075 I1076	A807 C808 C811 E813 C836 S998 C1074 I1075
BS04	TPP	A	P27 I28 E62 Q86 E814 G836 C837 F866 G966 D967 G968 V997 Y998 S999 N1000 T1001	P26 I27 E61 Q85 E813 G835 C836 F865 G965 D966 G967 V996 Y997 S998 N999 T1000
BS05	MG	A	D967 T995 V997	D966 T994 V996
BS06	COA	A	T29 S424 D425 V428 G429 R554 Y587 N1000	T28 S423 D424 V427 G428 R553 Y586 N999

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)