ROCA_GEOTN
ID ROCA_GEOTN Reviewed; 515 AA.
AC A4IJP9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=GTNG_0169;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO65553.1; -; Genomic_DNA.
DR RefSeq; WP_008881510.1; NC_009328.1.
DR AlphaFoldDB; A4IJP9; -.
DR SMR; A4IJP9; -.
DR STRING; 420246.GTNG_0169; -.
DR EnsemblBacteria; ABO65553; ABO65553; GTNG_0169.
DR KEGG; gtn:GTNG_0169; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000001578; 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.
FT CHAIN 1..515
FT /note="1-pyrroline-5-carboxylate dehydrogenase"
FT /id="PRO_1000045971"
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; 56574 MW; 07C58FFA56B656FD CRC64;
MVQPYKHEPF TDFTVDANRQ AFLAALEKVE AELGREYPLI IGGERVMTED KITSVNPANK
AEVIGRVAKA NKELAERAMK TADEAFRTWS RTSPEARADI LFRAAAIVRR RKHEFSAWLV
KEAGKPWREA DADTAEAIDF MEYYGRQMLK LKDGIPVESR PGETNRFFYI PLGVGVVISP
WNFPFAIMAG TTVAALVTGN TVLLKPASAT PVVAYKFAEV LEEAGLPAGV LNYIPGSGAE
VGDYLVEHPR TRFISFTGSR DVGIRIYERA AKVQPGQIWL KRVIAEMGGK DAIVVDKEAD
LELAAQSIVA SAFGFSGQKC SACSRAIIVE DVYDQVLNRV VELTKQLNVG DPAEQATFMG
PVIDQGAYNK IMEYIEIGKQ EGRLMTGGEG DDSKGFFIQP TVFADVDPNA RIMQEEIFGP
VVAFAKARDF DHALEIANNT QYGLTGAVIS RNRANLEKAR HEFHVGNLYF NRGCTGAIVG
YQPFGGFNMS GTDSKAGGPD YLILHMQAKT VSEMF