ROCA_STAEQ
ID ROCA_STAEQ Reviewed; 514 AA.
AC Q5HL59;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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}; OrderedLocusNames=SERP2128;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53020.1; -; Genomic_DNA.
DR RefSeq; WP_002438089.1; NC_002976.3.
DR AlphaFoldDB; Q5HL59; -.
DR SMR; Q5HL59; -.
DR STRING; 176279.SERP2128; -.
DR EnsemblBacteria; AAW53020; AAW53020; SERP2128.
DR KEGG; ser:SERP2128; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000531; 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..514
FT /note="1-pyrroline-5-carboxylate dehydrogenase"
FT /id="PRO_0000056521"
FT ACT_SITE 286
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
FT ACT_SITE 320
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00733"
SQ SEQUENCE 514 AA; 56876 MW; 99EE786D43629FF4 CRC64;
MVVPFKNEPG IDFSVQTNVE RFNEELRKVK AQLGQDIPLV INGEKLTKTD TFNSVNPANT
SQLIAKVSKA TQDDIEKAFE SANHAYQSWK KWSHKDRAEL LLRVAAIIRR RKEEISAIMV
YEAGKPWDEA VGDAAEGIDF IEYYARSMME LADGKPVLDR EGEHNRYFYK PIGTGVTIPP
WNFPFAIMAG TTLAPVVAGN TVLLKPAEDT VLTAYKLMEI LEEAGLPQGV VNFVPGDPKE
IGDYLVDHKD THFVTFTGSR ATGTRIYERS AVVQEGQQFL KRVIAEMGGK DAIVVDNNVD
TDLAAEAIVT SAFGFSGQKC SACSRAIVHQ DVHDEILEKA IQLTQKLTLG NTEENTFMGP
VINQKQFDKI KNYIEIGKKE GKLETGGGTD DSTGYFIEPT IFSGLQSADR IMQEEIFGPV
VGFIKVKDFD EAIEVANDTD YGLTGAVITN HREHWIKAVN EFDVGNLYLN RGCTAAVVGY
HPFGGFKMSG TDAKTGSPDY LLNFLEQKVV SEMF