Reviewed, UniProtKB/Swiss-Prot P39821 (PROA_BACSU)

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:	BSU13130

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the gamma-glutamyl phosphate reductase family.
Sequence caution	The sequence BAA05045.1 differs from that shown. Reason: Frameshift at position 375.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 415	415	Gamma-glutamyl phosphate reductase HAMAP MF_00412		PRO_0000189696
Experimental info
	Sequence conflict	108	1	E → Q in BAA05045. Ref.1
	Sequence conflict	174	1	A → T in BAA05045. Ref.1
	Sequence conflict	271	1	H → N in BAA05045. Ref.1
	Sequence conflict	359	1	A → R in CAA05592. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P39821-1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 9FB7B0C04C9F62D0	FASTA	415	45,252
	10 20 30 40 50 60 MSEVSVKAKL AKEAAAEMIM KTTAEKDEAL SLIANGLRKE LDFLLAENAK DIVNGKENGL 70 80 90 100 110 120 TPDIIDRLSL DEKRIRDIAD AVELLIDLAD PIGDSLETIE KENGLFIEKI RVPLGVVGMI 130 140 150 160 170 180 YEARPNVTVD AATLCLKTGN AVVLRGSSSA IHSNKALVSV IYRALEQSAL PIHAVQLIED 190 200 210 220 230 240 TSRETAKELF TLNDGLDVLI PRGGKKLIDL VVRESTVPVL ETGAGNCHIF IDETAKPQMA 250 260 270 280 290 300 EKVVVNAKTQ RPSVCNAIES LLIHKAWARQ HGKELLDQLE NAGVEIRGDE LVCELHPSSK 310 320 330 340 350 360 QASKEDWETE FLAPVLSVKT VENVQEAVKH IQQYGTNHSE AILTENDKNA VYFQTAVDAA 370 380 390 400 410 AVYHNASTRF TDGFEFGYGA EIGISTQKLH ARGPMGLPAL TSTKYIIKGT GQIRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis." Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T. J. Bacteriol. 176:5673-5680(1994) [PubMed: 8083159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Sequence of the Bacillus subtilis genome between xlyA and ykoR." Devine K.M. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 359.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D26044 Genomic DNA. Translation: BAA05045.1. Frameshift. AJ002571 Genomic DNA. Translation: CAA05592.1. AL009126 Genomic DNA. Translation: CAB13170.2.
PIR	C69682.
RefSeq	NP_389196.2.
3D structure databases
HSSP	HSSP built from PDB template 1O20 based on UniProtKB Q9WYC9.
ModBase	Search...
Genome annotation databases
GeneID	936166.
GenomeReviews	Gene locus BSU13130 in contig AL009126_GR.
KEGG	bsu:BSU13130.
NMPDR	fig|224308.1.peg.1315.
Organism-specific databases
SubtiList	BG10964. proA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P39821.
OMA	QYPAACN.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1315-MON.
BRENDA	1.2.1.41. 150.
Family and domain databases
HAMAP	MF_00412. [Tree]
InterPro	IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. 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. 1 hit.
PANTHER	PTHR11063:SF1. GSA_DH. 1 hit.
PIRSF	PIRSF000151. GPR. 1 hit.
TIGRFAMs	TIGR00407. proA. 1 hit.
PROSITE	PS01223. PROA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PROA_BACSU

Accession

Primary (citable) accession number: P39821
Secondary accession number(s): O35032

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	June 16, 2009
Last modified:	November 3, 2009
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)