Q9HHA1 (PROA_METAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-glutamyl phosphate reductase
Short name=GPR
EC=1.2.1.41

Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Short name=GSA dehydrogenase

Gene names

Name:	proA
Ordered Locus Names:	MA_4100

Organism

Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

Taxonomic identifier

188937 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. HAMAP MF_00412
Catalytic activity	L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH. HAMAP MF_00412
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2. HAMAP MF_00412
Subcellular location	Cytoplasm By similarity HAMAP MF_00412.
Sequence similarities	Belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamate-5-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189821

Sequences

	Sequence		Length	Mass (Da)
	Q9HHA1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 1DB82A991E4E075F	FASTA	447	49,360
	10 20 30 40 50 60 MAEDIETKVV KAKKASIELS SVSEEVKNRA LEAMAESLDR ERKAILEANS KDLEYASELK 70 80 90 100 110 120 KVGKLTQALV DRLKVTDSKI DGMIAGIMDV IKLKDPVGET LSTLELDNDL ILYQISCPIG 130 140 150 160 170 180 LIGVIFESRP DVVPQVMSLC LKSGNATIFK GGSEARESNR TIFEILVKAI ESTEGMPKGA 190 200 210 220 230 240 FQLMETREEI MSLLSLDAYV DLLIPRGSNE FVKFIQDNTK IPVLGHTSGI CHIYVDEFAD 250 260 270 280 290 300 PDTAWKVCFD AKVQYPAVCN AIETLLVNRK IAEAFLPKMA EMYIKAGVEL RCDKDSYILL 310 320 330 340 350 360 AEKGLSPLSK ATEEDWSLEY NDLILSIKLV DTIKEAIAHI NTFGSHHTDG IITENASRRK 370 380 390 400 410 420 EFIGLVDSSS VMVNASTRFA DGYRYGKGAE VGISTNKIHS RGPVGMEGLL IYKYILMGKG 430 440 QVVADYAGEN AKPYTHRKLD LKFADVN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Directed mutagenesis and plasmid-based complementation in the methanogenic archaeon Methanosarcina acetivorans C2A demonstrated by genetic analysis of proline biosynthesis." Zhang J.K., White A.K., Kuettner H.C., Boccazzi P., Metcalf W.W. J. Bacteriol. 184:1449-1454(2002) [PubMed: 11844777] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
[2]	"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity." Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P. , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B. Genome Res. 12:532-542(2002) [PubMed: 11932238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF305580 Genomic DNA. Translation: AAG22031.1. AE010299 Genomic DNA. Translation: AAM07448.1.
RefSeq	NP_618968.1. NC_003552.1.
3D structure databases
ProteinModelPortal	Q9HHA1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1475994.
GenomeReviews	Gene locus MA_4100 in contig AE010299_GR.
KEGG	mac:MA4100.
NMPDR	fig|188937.1.peg.3994.
Phylogenomic databases
HOGENOM	HBG318080.
OMA	QYPAACN.
ProtClustDB	PRK00197.
Enzyme and pathway databases
BioCyc	MACE188937:MA4100-MONOMER.
Family and domain databases
HAMAP	MF_00412. ProA. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR000965. G-glutamylP_reductase. IPR020593. G-glutamylP_reductase_CS. IPR012134. Glu-5-SA_DH. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits.
KO	K00147.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF000151. GPR. 1 hit.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00407. ProA. 1 hit.
PROSITE	PS01223. PROA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROA_METAC

Accession

Primary (citable) accession number: Q9HHA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	March 1, 2001
Last modified:	November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program