ID G6FYX4_9CYAN Unreviewed; 1025 AA.
AC G6FYX4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=FJSC11DRAFT_4073 {ECO:0000313|EMBL:EHC09436.1};
OS Fischerella thermalis JSC-11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Hapalosiphonaceae;
OC Fischerella.
OX NCBI_TaxID=741277 {ECO:0000313|EMBL:EHC09436.1, ECO:0000313|Proteomes:UP000004344};
RN [1] {ECO:0000313|EMBL:EHC09436.1, ECO:0000313|Proteomes:UP000004344}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-11 {ECO:0000313|EMBL:EHC09436.1,
RC ECO:0000313|Proteomes:UP000004344};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Sarkisova S., Bryant D.A., Brown I.,
RA Woyke T.J.;
RT "The draft genome of Fischerella sp. JSC-11.";
RL Submitted (SEP-2011) 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:EHC09436.1}.
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DR EMBL; AGIZ01000014; EHC09436.1; -; Genomic_DNA.
DR AlphaFoldDB; G6FYX4; -.
DR PATRIC; fig|741277.3.peg.3557; -.
DR Proteomes; UP000004344; 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:UP000004344}.
FT DOMAIN 11..126
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 135..441
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 549..1009
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 785
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 819
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1025 AA; 113747 MW; 3F1A840DD0BEA62A CRC64;
MVLQVKTSAY EAKTQEIAKI LLGVTQENRN FFSALRDQMR WDDRILAWAM SNPGLRVQLF
RFIDTLPALH SKSEIAAHLQ EYLGDETVEL PSALKGMLNF ANPDSMPGQV AATTVATAVE
TLAHRYIAGE NIKQVLKTIE RLRKDKMAFT VDLLGEAVIT EAEAQSYLER YLDLMQQLAE
AAKNWATVPL IDQADGEPLP KVQVSVKLTA FYSQFDSLDP QGSEARVSDR IRILLRRAKE
LGVAVHFDME QYEYKDLIFN ILKKLLLEEE FRARTDIGMT IQAYLRDSEQ DAKALIDWAK
ERGYPMTIRL VKGAYWDQET IKAEQKHWPQ PVYNDKAATD ANFENITQLL LENHQYVYAA
IGSHNVRSQA HAIAIAQSLK VPSRCFEMQV LYGMGDKLAK ALVDQGYRVR VYCPYGELLP
GMAYLIRRLL ENTANSSFLR QNLENRPVEE LLAPPTFKQE DKEKVARGDG RRELVATDTD
DKVARGEGRR EFRTLEENGK TAVKFVGAAD TDYAEEESRK ESQQALQTVR QQLGKTYLPL
INGEYVNTQE MINSVNPSNY TEVVGKIGLS SVEQAEQAMQ AAKAAFPSWR KTPVQQRAGI
LYKAADLMEQ RRAELAAWIV LEVGKTVREA DAEVSEAIDF CRYYAMEMER LEQGYNYDVA
GETNRYIYQP RGIAVVISPW NFPLAIATGM TVAALVAGNC TLLKPAETSS VIAAKLTEVL
VDAGIPKGVF QYVPGKGSQV GAYLVNHIDT HVIAFTGSQE VGCRIYAEAA NLKPGQKHMK
RVIAEMGGKN AIIVDESADL DQAVMGVVQS AFGYSGQKCS ACSRVIVHTA IYDSFVRRFT
EATKSLNIGA AELPGTKVGP VIDANARDRI REYIEKGKAE AKVALEMPAP ENGYFIGPVI
FTDVSPNAVI AQQEIFGPVV AVIKANNFQE ALSIANSTNY ALTGGLYSRT PSHIQKAQED
FEVGNLYINR TITGAIVARQ PFGGFKLSGV GSKAGGPDYL LQFLEPRTIT ENIQRQGFAP
IEGAE
//
