ID A0A0M2HFH0_9MICO Unreviewed; 1243 AA.
AC A0A0M2HFH0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN Name=rocA {ECO:0000313|EMBL:KJL42987.1};
GN ORFNames=RS81_00951 {ECO:0000313|EMBL:KJL42987.1};
OS Microbacterium ketosireducens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=92835 {ECO:0000313|EMBL:KJL42987.1, ECO:0000313|Proteomes:UP000033956};
RN [1] {ECO:0000313|EMBL:KJL42987.1, ECO:0000313|Proteomes:UP000033956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12510 {ECO:0000313|EMBL:KJL42987.1,
RC ECO:0000313|Proteomes:UP000033956};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:0000256|ARBA:ARBA00001468};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJL42987.1}.
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DR EMBL; JYIZ01000039; KJL42987.1; -; Genomic_DNA.
DR RefSeq; WP_045274920.1; NZ_JYIZ01000039.1.
DR AlphaFoldDB; A0A0M2HFH0; -.
DR STRING; 92835.RS81_00951; -.
DR PATRIC; fig|92835.4.peg.970; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000033956; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:InterPro.
DR Gene3D; 3.20.20.220; -; 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; IPR025703; Bifunct_PutA.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR PIRSF; PIRSF000197; Bifunct_PutA; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000033956}.
FT DOMAIN 131..419
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 584..1006
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 790
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 824
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1243 AA; 132406 MW; 772FD26A630BFA00 CRC64;
MNENPESSTA SADEAVALAK RWIAESAEVE ADPAAERLAG VLKDGNGLPF TIGFVDGVMR
PESLSAAASN LQRVAPLVPD FLPWYLRTAV RVGGAVAPVL PMPVVPIARR VLREMVGHLI
VDARPDKLGP AIAQLRESGA RLNLNLLGEA VLGEKEALRR LDGIHELIRR DDVDYVSVKV
SAIASHISMW AFDEVVDTVI ERLLPLYLTA AANGTFINLD MEEYRDLDLT IAVFTRILDD
PRLRLLEGGI VLQAYLPDAQ PALERLTAWA QDRVAAGGAR IKVRLVKGAN LAMEHVDAVM
HGWSLATYDA KVDSDANYLR CLRFALRPEN TAAVRLGVAG HNLFDIAYAW LLAGERGVQA
DVEVEMLLGM AQGQVEAVTR EVGHVLLYVP VVRPDEFDVA ISYLVRRLEE NASSENFLSA
AFELADDPVL LVRERDRFLA SLARADDPEL SIGAHRHQDR AAEAAALAAG TDEKQRLRTR
ARGGDESGLT QAVIGIARSA VAGDEILQRE PGETAPVAPT VEEQLFGGAR FVETAVFAPR
EGAERAAGAP GFHNAPDSDP ALPANRAWAR GILSRVEHST AGDATVAASR LSDIAAVDAV
VARVGAAAAA WGARPAAERG DVLAAAGRAL EARRAELIEV AASETGKVFA EADVEVSEAV
DFAHYYAATA RELDRVSGAV FEPALVTVVT PPWNFPVAIP SGGVLAALAA GSGVVFKPAP
QARRCAAVVA EALWDAGVPR DVLALVDIDE GSLGQALVSH DDVDRVILTG SYETAALFRS
WRPELPLLAE TSGKNAMIVM PSADLDLAAG DVIKSAFGHA GQKCSAASLV ILVGPVGHSQ
RFARQLVDAA SSLRVGPPSD PLSEVGPVIE PPHGKLAWAL STLDEGEQWL VEPRRLDAGP
ELAGRMWSPG IRVGVQPGSR FHQEEFFGPV LGVMHASSLS QAIELQNAVA YGLTAGLYTQ
NPEDLEVWLD RVEAGNLYVN RGITGAIVQR QPFGGWKRSS VGAGAKAGGP NYLVGLGSWR
ASAGGQSSST TLHLRGLDSR IAGVIEAAQP SLDYEAFEWL RRGALSDAIA WDREFGQVRD
VSALGVERNL FRYRPVGEVA VRATADASWQ ALLRVIVAGV RAGAVLTVSA PVGLPAGVRR
ALTEQDVPVF VESDAQWIER MQLPAADGSD RSARARLVGS RSSVAQLHRA LAAATGGDPD
LAVYDADVTT AGRLELLPFL REQSITITAH RFGNPDRWSE AVI
//
