ROCA_ANOFW
ID ROCA_ANOFW Reviewed; 515 AA.
AC B7GFV3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Aflv_0249;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ32633.1; -; Genomic_DNA.
DR RefSeq; WP_012573970.1; NC_011567.1.
DR AlphaFoldDB; B7GFV3; -.
DR SMR; B7GFV3; -.
DR STRING; 491915.Aflv_0249; -.
DR EnsemblBacteria; ACJ32633; ACJ32633; Aflv_0249.
DR KEGG; afl:Aflv_0249; -.
DR PATRIC; fig|491915.6.peg.254; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_0_9; -.
DR OMA; NWNKQLT; -.
DR OrthoDB; 744602at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000000742; 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_1000132748"
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; 56735 MW; 740FDEADC2C72C0D CRC64;
MVQPYKHEPF TDFTVEANKK AFEEGLKTVQ AYLGQDYPLV IGGERVMTED KIVSINPANK
TEVVGRVAKA NKDLAEKAMQ TADAAFKWWS KTKPEMRADI LFRAAAIVRR RKHEFSALLV
KEAGKPWKEA DADTAEAIDF MEYYARQMLK LKDGIPVESR PGETNRFFYI PLGVGVVISP
WNFPFAIMAG TTVAALVTGN TVLLKPASAT PVVAYKFVEV LEEAGLPAGV LNYIPGSGAE
VGDYLVDHPR TRFISFTGSR DVGIRIYERA AKVHPGQIWL KRVIAEMGGK DTIVVDKEAD
LELAAQSIVA SAFGFSGQKC SACSRVVALE DVYDQVLNRV VELTKQLKVG NPEEQSTFMG
PVIDQSAYNK IMEYIEIGKQ EGKLMTGGEG DDSKGFFIQP TVFADLDPKA RIMQEEIFGP
VVAFTKAKDF DHALEIANNT EYGLTGAVIS NNRFNLEKAR EEFHVGNLYF NRGCTGAIVG
YHPFGGFNMS GTDSKAGGPD YLLLHMQAKT VSEMF