ID K9ULL5_CHAP6 Unreviewed; 1012 AA.
AC K9ULL5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=Cha6605_5097 {ECO:0000313|EMBL:AFY95997.1};
OS Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC Chamaesiphon.
OX NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY95997.1, ECO:0000313|Proteomes:UP000010366};
RN [1] {ECO:0000313|EMBL:AFY95997.1, ECO:0000313|Proteomes:UP000010366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Chamaesiphon sp. PCC 6605.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; CP003600; AFY95997.1; -; Genomic_DNA.
DR RefSeq; WP_015162084.1; NC_019697.1.
DR AlphaFoldDB; K9ULL5; -.
DR STRING; 1173020.Cha6605_5097; -.
DR KEGG; cmp:Cha6605_5097; -.
DR PATRIC; fig|1173020.3.peg.5839; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005682_2_0_3; -.
DR OrthoDB; 548310at2; -.
DR Proteomes; UP000010366; 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; 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000010366}.
FT DOMAIN 22..140
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 149..454
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 535..994
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 771
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 805
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1012 AA; 111834 MW; AF702756F03CC44F CRC64;
MVNSTQQVHS QFDTNLDIAK YESKTQEIAR QLLGETTKSS IWSKLSQIKD ELRFDDKLMA
WTMENEGLRV QLFRLIDCLP ALQSKAEIAR HMQEYLANDA VEVPAMRSLL NFSTDNPNSL
TATAAATTLS TAIATLAKRY ICGENLPAAT KTIERLRRER LAFTMDLLGE AVISEVEAEG
YLDRYLTMME NLAARARNWP TIAEIDRSEL GSLDRVQVSV KLSAFYSQFD PLDPVMTTEK
VSEPVRRLLR KAQAIGCGIH FDMEQYEFKS LTLQILKQVL MEPEFVDRTN VGLTIQGYLR
DSEADLYDLI AWAKERAHPV TVRLVKGAYW DRETIRAYQQ GWAIPVFSDK VSTDANYERL
TQILLENHQY LHAAIGSHNA RSLAKAIAIV QTLNIPSSSF EVQCLYGMGD EFAKKIVDLG
YRVRIYCPFG ELIPGMSYLI RRLLENTANS SFLRMSSSES RAISELVAAP VMTDRDRLDK
GTLATTSFEG FTNASDRDYA IERQRTAAQT ALQTVRDRLG KTYLPIIDDR PVQTEEYIES
VNPANSAQVV GKIGLASIEQ ADAAVKSAKN AWTTWKQLSA RHRGDILRKA ADLMEAQRDE
LTAWITWEVA KPIREGDAEV SEAIDFCRYY AREMERLESG VQRNLPGEDN TYIYQPRGVV
VVISPWNFPL AIALGMSVAA IAAGNTVILK PAEQSSVIGA KIAEILHAAG LPPGVFTYLP
AKGSTVGAHL VKHPDVHLIA FTGSQQVGCQ IVAEAAILRP KQKHMKRVIA EMGGKNGIII
DESADLDQAV VGVMNSTFGF AGQKCSACSR AIVLAPVYDN FLDRLVAATR SLKVGAAHHA
DTKLSAVIDA AAQANIQRYI EIGKESAKLA LSMPVPEGGY YVSPTIFSEV DPDSTIAQEE
IFGPVLAVIK AENFDEALEI ANGTNFALTG GLYSRTPSHI DRAYREFEVG NLYINRGITG
ALVDRHPFGG FKLSGVGSKA GGRDYLLQFL EPRSITENTQ RQGFAPGDIS MN
//
