ID E0DIR6_9CORY Unreviewed; 1147 AA.
AC E0DIR6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=HMPREF0299_5579 {ECO:0000313|EMBL:EFM47794.1};
OS Corynebacterium matruchotii ATCC 14266.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=553207 {ECO:0000313|EMBL:EFM47794.1, ECO:0000313|Proteomes:UP000004218};
RN [1] {ECO:0000313|EMBL:EFM47794.1, ECO:0000313|Proteomes:UP000004218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14266 {ECO:0000313|EMBL:EFM47794.1,
RC ECO:0000313|Proteomes:UP000004218};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFM47794.1}.
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DR EMBL; ACSH02000008; EFM47794.1; -; Genomic_DNA.
DR RefSeq; WP_005527028.1; NZ_ACSH02000008.1.
DR AlphaFoldDB; E0DIR6; -.
DR STRING; 553207.HMPREF0299_5579; -.
DR GeneID; 84575139; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000004218; Unassembled WGS sequence.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:InterPro.
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:UP000004218}.
FT DOMAIN 144..434
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 520..935
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 474..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 721
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 755
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1147 AA; 125434 MW; 11C55DEF947FA636 CRC64;
MTDAYTPLPN SSDLDKAAEA AVIRAKEWLA LTNNAASKKE AASTEQLAAL VRDDDGIRFT
MGFVDRVARP TDNKVAAHEL SSLANPFKTA IPSFIGAVDK GLVSVGAVAA PIFPSLVMPL
ARKRLRQMVS HLVLDAEGKA LNAKLTEAKE QGYQLNLNLL GEAVLGEAEA KSRLERTRQM
LQNPLVTYAS IKASSVCAQL NPWDIQGNIE RLKDRLRPLY REAMKRSPHA FINMDMEEYK
DLRLTIDLFK DLLSEDEFMP LEAGIVLQAY LPDTFDALVE LAEFAKERRA KGGAKIKIRL
VKGANLSMER VEAQLHDWAQ APYLSKEDVD ANYYRLMDYI FQPEHADNVR IGIASHNLFT
VALATKLVEL RGVQHQLDVE MLQGMAPAQA RAVHEVVGGL ILYTPVVHAE DFDVAVSYLV
RRLEENGEKH NFLHALFAHD PQPMEDQEQH FLNAVRDRWD TFAGPRRTQD RITDKGLQSG
TVPGHFLGEP DTDPSLPQNR DWALALLKKD PGKVESPKVT DPAQIDKVVA TAQKQSAAWA
KLSGKERAEV LTSIATELAN ARGDLINVMT HESGKTVGES DPEISEAIDF AMYYAESARQ
LDVARSKFTP FKVVLVTPPW NFPVAIPMGG VFAALAAGAA VIIKPAPQVV RCAEVAIKAV
HKALKGAGVD PALVQLVNAD EAEAGKHLVS HKDVDSVILT GASDTARLFR SWKPKMVLNA
ETSGKNAIIV TPSADPDLAV ADVYKSAFGH AGQKCSAASL VILVGSVGKS ERFINQLVDA
TRSLKVGKGT EIDTTMNGII EAPGEKLMRG LTQLEPGEQW LVKPEKLNEE GTLWSPGIRD
NVKPGSWYHT HECFGPVLGI MRADTLEEAI KLQNSTGFGL TGGIHSLDQD EIDYWRENVE
VGNAYVNRGI TGAIVERQSF GGWKDSAIGS GAKAGGPNYV AQQGVWADGD LSQVPSVSLD
PAINRALRDI LSTVELSDED REWLQKAAHL DALAWREEFN VEHDRTALLC ETNVFRYRPL
LQPLQVRIGA DFKLRDVLRL QLAALITESP VRFSANQDTA VALAKAGIKV DVVSDADFAA
EIRKDSGVRI RTVGKVSDDL YPAAAESSSV VLDQPVLADG RRELLPFLLE QAVATTQHRF
GVIGKKI
//
