ID A0A2T1M287_9CHRO Unreviewed; 989 AA.
AC A0A2T1M287;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN Name=pruA {ECO:0000313|EMBL:PSF38864.1};
GN ORFNames=C7H19_02060 {ECO:0000313|EMBL:PSF38864.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF38864.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF38864.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF38864.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF38864.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF38864.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) 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:PSF38864.1}.
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DR EMBL; PXOH01000002; PSF38864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1M287; -.
DR OrthoDB; 548310at2; -.
DR Proteomes; UP000239001; 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 CDD; cd07124; ALDH_PutA-P5CDH-RocA; 1.
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 InterPro; IPR041514; PutA_N.
DR InterPro; IPR005932; RocA.
DR NCBIfam; TIGR01237; D1pyr5carbox2; 1.
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 Pfam; PF18083; PutA_N; 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:UP000239001}.
FT DOMAIN 12..127
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 137..442
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 513..972
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 749
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 783
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 989 AA; 110153 MW; B99DE67136DDCCF4 CRC64;
MVIQIDSNQT YEAKTQEIAK QLLAETRQKR SLWAQLQDQM RWDDKLLAWT MSNPNLRVQM
FRFIDCLPAL RSKGEIANHL QQYLGDESVE LPAALKGVLN FTDPNTPPAQ LAATTISKAV
ETLALKYIAG EDIGQITKTV ERLRSLKMAF TIDLLGEAVI TETEAKDYLQ AYLDLMQHLS
QQAKKWSKVP EIDEADGEPL PQIQVSVKLT AFYSQFDSFD PEGSKAKVCD RIRILLRRAE
ELGSAVHFDM EQYKYKDLTI SILQDLLLEE EFRTRTNIGV TLQAYLKDSE QDLKNWIEWA
KKRGYPITIR LVKGAYWDQE TIKSLQNHWP QPVYNDKAET DLNFERMTRL LLENHQYLYA
AIGSHNVRSQ SLACAIAETL NIPRRRFEMQ VLYGMGDQLA KALVKRGHRV RVYSPYGDLL
PGMAYLIRRL LENTANSSFL RQNLEERPID ELIAPPKVGN ASQPISNGYP NAPDTDYANS
DLRNQAEKAL VQVRGELGKT YKPLINGEYI NTNQTVDSVN PSNPSELIGL LGLLSVEQAE
IALKSAKEAF TAWKKTPVRV RAGILRKAAE IMEKRRHELN AWICLEVGKV IQQADAEVSE
AIDFCRYYAD EMERLDQGYV LDVAGETNRY IYQPRGIALV ISPWNFPFAI AVGMTVAALV
TGNCTLLKPA ETSSIIAAKI TEILIDAGIP KGVFQFVPGK GSEVGAYMVK HPDVHLIAFT
GSREVGCRIY ADAAILQPRQ KHLKRVIAEM GGKNAIIVDE SADLDQAVAG VVYSAFGYSG
QKCSACSRVI VLDPVHDAFV ERFVEATKSL NIGPTDLPST QVGPVIDATA QARIKEYIAK
GKTESEVALE REAPENGYFV GPTIFKNVSA NATIAQEEIF GPVVAVIRVK NFDEALQVAN
GTDYALTGGL YSRTPEHIER ANAEFEVGNL YINRGITGAI VSRQPFGGFK LSGVGSKAGG
PDYLLQFLEP RHISENIQRQ GFAPIEGVD
//
