Structure of PDB 3haz Chain B

Receptor sequence

>3hazB (length=974) Species: 224911 (Bradyrhizobium diazoefficiens USDA 110)

PNIPPPFTAPYAPDDAEIAARLLPASHLSPPQEARIHRTATRLIEAIRKL
GGVEDMLREFALSTKEGLALMVLAEALLRVPDARTADQFIEDKLGEGDFI
HHETKSTAFLVNASAWARVIQPGETPDGTIGRLVKRLGAPAVRTATRQAM
RLMGNHFVLGETIEQALERGKPRSGQKTRYSFDMLGEGARTAADARRYFD
AYASAIETIGKAAGNHALPDRPGISVKLSALHPRFEAISRARVMVELVPQ
LLDLAQRAKAHDLNFTVDAEEADRLELSLDVIAATLADPSLKGWDGFGLA
IQAYQKRASAVIDYVDALARAHDRKLMVRLVKGAYWDTEIKRAQERGLDG
YPVFTRKAMTDLNYVACASKLLALRPRIFPQFATHNALTVATVLEMAEGS
SGFEFQRLHGMGEALYEQLAKDHADIAYRTYAPVGSHRDLLAYLVRRLLE
NGANSSFVAQAADYRVPVPALLQRPADAIVRPQAAAHPRIPLPCDLFAPE
RRNSRGVEFGARTALDQLLTDVKAETIADATPDQAHAAVAAARAGFAGWS
RTPAGIRAAALEQAAHLLESRSAHFIALLQREGGKTLDDALSELREAADF
CRYYAAQGRKLFGSETAMPGPTGESNALTMRGRGVFVAISPWNFPLAIFL
GQVTAALMAGNSVVAKPAEQTPRIAREAVALLHEAGIPKSALYLVTGDGR
IGAALTAHPDIAGVVFTGSTEVARSINRALAAKDGPIVPLIAETGGINAM
IADATALPEQVADDVVTSAFRSAGQRCSALRLLFVQEDVADRMIEMVAGA
ARELKIGDPSDVATHVGPVIDVEAKQRLDAHIARMKTEARLHFAGPAPEG
CFVAPHIFELTEAGQLTEEVFGPILHVVRYRPENLERVLRAIERTGYGLT
LGVHSRIDDSIEAIIDRVQVGNIYVNRNMIGAVVGVQPFGGNGLSGTGPK
AGGPHYLARFATEQTVTINTAAAG

3D structure

• PDB: 3haz Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum
• Chain: B
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N658 K681 E758 C792 E884 A966
• Catalytic site (residue number reindexed from 1): N643 K666 E743 C777 E869 A951
• Enzyme Commision number: 1.2.1.88: L-glutamate gamma-semialdehyde dehydrogenase.
  1.5.5.2: proline dehydrogenase.

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	FAD	B	D278 A279 Q312 R339 V341 K342 G343 A344 Y345 W346 F364 T365 R366 K367 T370 A393 T394 H395 N396 R417 Y441 S466 F467	D268 A269 Q302 R329 V331 K332 G333 A334 Y335 W336 F354 T355 R356 K357 T360 A383 T384 H385 N386 R407 Y431 S456 F457
BS02	NAD	B	I654 S655 P656 W657 N658 I663 K681 P682 A683 G714 G717 A718 T732 G733 S734 V737 I741 E758 T759 C792 E884 F886 F954	I639 S640 P641 W642 N643 I648 K666 P667 A668 G699 G702 A703 T717 G718 S719 V722 I726 E743 T744 C777 E869 F871 F939

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003677 DNA binding
• GO:0003700 DNA-binding transcription factor activity
• GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity
• GO:0004657 proline dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
• GO:0042802 identical protein binding

Biological Process

• GO:0006355 regulation of DNA-templated transcription
• GO:0006560 proline metabolic process
• GO:0006561 proline biosynthetic process
• GO:0006562 proline catabolic process
• GO:0010133 proline catabolic process to glutamate

Cellular Component

• GO:0009898 cytoplasmic side of plasma membrane

External links

• PDB: RCSB:3haz, PDBe:3haz, PDBj:3haz
• PDBsum: 3haz
• PubMed: 20133651
• UniProt: Q89E26