ROCA_BACAN
ID ROCA_BACAN Reviewed; 515 AA.
AC Q81ZF8; Q6I4A5; Q6KY08;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=1-pyrroline-5-carboxylate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
DE Short=P5C dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
DE EC=1.2.1.88 {ECO:0000255|HAMAP-Rule:MF_00733};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00733};
GN Name=rocA {ECO:0000255|HAMAP-Rule:MF_00733};
GN OrderedLocusNames=BA_0309, GBAA_0309, BAS0295;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00733};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_00733}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. RocA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00733}.
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DR EMBL; AE016879; AAP24344.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29396.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52626.1; -; Genomic_DNA.
DR RefSeq; NP_842858.1; NC_003997.3.
DR RefSeq; WP_000259550.1; NZ_WXXJ01000007.1.
DR AlphaFoldDB; Q81ZF8; -.
DR SMR; Q81ZF8; -.
DR IntAct; Q81ZF8; 1.
DR STRING; 261594.GBAA_0309; -.
DR DNASU; 1087266; -.
DR EnsemblBacteria; AAP24344; AAP24344; BA_0309.
DR EnsemblBacteria; AAT29396; AAT29396; GBAA_0309.
DR GeneID; 64202466; -.
DR KEGG; ban:BA_0309; -.
DR KEGG; bar:GBAA_0309; -.
DR KEGG; bat:BAS0295; -.
DR PATRIC; fig|198094.11.peg.299; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OMA; NWNKQLT; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00733; RocA; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005932; RocA.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01237; D1pyr5carbox2; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..515
FT /note="1-pyrroline-5-carboxylate dehydrogenase"
FT /id="PRO_0000056503"
FT ACT_SITE 286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT ACT_SITE 320
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT CONFLICT 168
FT /note="S -> F (in Ref. 3; AAT52626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56225 MW; 13A0909998818332 CRC64;
MVVAYKHEPF TDFSVEANKL AFEEGLKKVE SYLGQDYPLI IGGEKITTED KIVSVNPANK
EELVGRVSKA SRELAEKAMQ VADETFQTWR KSKPEMRADI LFRAAAIVRR RKHEFSAILV
KEAGKPWNEA DADTAEAIDF MEYYGRQMLK LKDGIPVESR PIEYNRFSYI PLGVGVIISP
WNFPFAIMAG MTTAALVSGN TVLLKPASTT PVVAAKFMEV LEEAGLPAGV VNFVPGNGSE
VGDYLVDHPR TRFISFTGSR DVGIRIYERA AKVNPGQIWL KRVIAEMGGK DTIVVDKEAD
LELAAKSIVA SAFGFSGQKC SACSRAVIHE DVYDHVLNRA VELTKELTVA NPAVLGTNMG
PVNDQAAFDK VMSYVAIGKE EGRILAGGEG DDSKGWFIQP TIVADVAEDA RLMKEEIFGP
VVAFCKAKDF DHALAIANNT EYGLTGAVIS NNRDHIEKAR EDFHVGNLYF NRGCTGAIVG
YQPFGGFNMS GTDSKAGGPD YLALHMQAKT TSETL
