ID A0A1Y0RLC3_9CYAN Unreviewed; 995 AA.
AC A0A1Y0RLC3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=BZZ01_08310 {ECO:0000313|EMBL:ARV58639.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV58639.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV58639.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV58639.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-2017) 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}.
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DR EMBL; CP019636; ARV58639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RLC3; -.
DR KEGG; ncn:BZZ01_08310; -.
DR OrthoDB; 548310at2; -.
DR Proteomes; UP000196302; Chromosome.
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:UP000196302}.
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 520..979
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 755
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 789
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 995 AA; 110009 MW; D708FD71851C4E5A CRC64;
MVLQVKTSTY EAKTQEIAKQ LLAATQENRS FFGALREQMR WDDKLLAWAM SNPGLRVQLF
RFIDTLPALR SKPEIAAHLQ EYLGDESVEL PAALKGMLNF ANPDSMPGQV AATTVSTGVE
TLAHKYISGE NIKQALKTIE RLRKEKMAFT VDLLGEAVIT EAEAQSYLQR YLDLMQQLVD
ASKSWTPVPL IDEADGQPLP KVQVSVKLTA FYSQFDPLDA KGSEERVSDR IRILLRRAKE
LGASVHFDME QYAYKDLIFS ILKKLLMEEE FRTRTDIGMT IQAYLRGSEQ DARDLIAWAK
QRGYPVTIRL VKGAYWDQET IKAEQKHWQQ PVYNDKVATD ANFEVITQLL LENYEYVYSA
IGSHNVRSQA HAIAIADSLN VPRRSFEMQV LYGMGDKIAK ALVDRGYRVR VYCPYGELLP
GMAYLIRRLL ENTANSSFLR QNMENRPVEE LLAPPVVESI SVASPSLAEG TEEGFSGAAD
TDYAEEEERR KAAQAFQAVR QQLGNTYLPL INGEYTNTEV FIDSVNPSNF SEVVGKVGLI
SVEQAEQAMQ AAKAAFPGWR KTPARERAGI LHKAADLMEQ RRAELSAWIV LEVGKPVREA
DAEVSEAIDF CRYYADEIER LDQGYNYDVA GETNRYIYQP RGIAVVISPW NFPLAIATGM
TVAALVTGNC TLLKPAETSS VIAAKLTEVL VDAGIPKGVF QYVPGKGSQV GAYLVNHPDT
HVIAFTGSQE VGCRIYAEAA ILKPGQKHMK RVIAEMGGKN AIIVDESADL DQAVVGVVQS
AFSYSGQKCS ACSRVVVLEP IYDNFVQRFV EATKSLNIGA TELPSTQVGP VIDANAYSRI
REYIEKGKAE AKVALEMPAP DNGYFIGPVV FTDVSPNAII AQQEIFGPVV AVIKVKNFKE
ALDVANGTNY ALTGGLYSRT PSHIEKAQEE FEVGNLYINR NITGAIVARQ PFGGFKLSGV
GSKAGGPDYL LQFLEPRTVT ENIQRQGFAP IEGAE
//
