ROCA_OCEIH
ID ROCA_OCEIH Reviewed; 515 AA.
AC Q8ERF4;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=OB1349;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13305.1; -; Genomic_DNA.
DR RefSeq; WP_011065755.1; NC_004193.1.
DR AlphaFoldDB; Q8ERF4; -.
DR SMR; Q8ERF4; -.
DR STRING; 221109.22777031; -.
DR EnsemblBacteria; BAC13305; BAC13305; BAC13305.
DR KEGG; oih:OB1349; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OMA; LMVMRET; -.
DR OrthoDB; 744602at2; -.
DR PhylomeDB; Q8ERF4; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000822; 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_0000056513"
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 515 AA; 57295 MW; 14B272164951F531 CRC64;
MVLPFKHEPF TDFTVKENRK DYQDALAKVK EELGKDYPLV INGEKIYTDD KLISINPSNK
NEVVGNVSKA TKQHIEEAFT SAKEAFKEWK SWSAEDRARV LYRAAAIVRR RKHEFSAWLS
YDAGKPWDQA DGDTAEGIDF LEYYARHMVE LEKGKPLADR PNEDNKYFYQ PLGPGVVIPP
WNFAFAIVCG TTVAPIVAGN PVLLKPSENT PVIAYKLVEV LEEAGLPKGV LNFVPGDPAE
IGDYLVDHKD THFINFTGSR ATGVRIFERA TKIQDGQTHL KRIVAEMGGK DTIIVDESAD
LDLAAESIVH SAFGFSGQKC SACSRAVIHE SVYDEVIEKS VELAKTLTVG NPTEDNVYMA
SVVNQKQFDK IKDYIEVGKQ EGELVFGGET DDNKGFFVHP TIFKDLDPKA RIMQEEIFGP
VVAFSKAKSF DELLDIANNT EYGLTGAVIS NNRENLNRAQ TEFLVGNLYF NRGCTAAIVG
YQPFGGFKMS GTDSKAGGPD YLQHFLNAKV VTERF