ID A0A2A2TIJ5_9CYAN Unreviewed; 998 AA.
AC A0A2A2TIJ5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:PAX53801.1};
GN ORFNames=CK510_13345 {ECO:0000313|EMBL:PAX53801.1};
OS Calothrix elsteri CCALA 953.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=987040 {ECO:0000313|EMBL:PAX53801.1, ECO:0000313|Proteomes:UP000218238};
RN [1] {ECO:0000313|EMBL:PAX53801.1, ECO:0000313|Proteomes:UP000218238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 953 {ECO:0000313|EMBL:PAX53801.1,
RC ECO:0000313|Proteomes:UP000218238};
RA Gagunashvili A.N., Elster J., Andresson O.S.;
RT "Draft genome sequence of filamentous cyanobacterium Calothrix elsteri
RT CCALA 953.";
RL Submitted (AUG-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 -!- 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:PAX53801.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NTFS01000130; PAX53801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2TIJ5; -.
DR OrthoDB; 548310at2; -.
DR Proteomes; UP000218238; 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; 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:UP000218238}.
FT DOMAIN 11..127
FT /note="Proline utilization A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18083"
FT DOMAIN 136..442
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 523..982
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 758
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 792
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 998 AA; 110210 MW; 05FC755A038B0219 CRC64;
MVLQVETNVY EAKTQEIAKQ LLAATQENRS FLGNLRDQMR LDDKLLDWAM SNPGLRVQLF
RFIDTLPALK NDKSEIAAHL QEYLGDDSVE LPNALKGMLN FASPDSMPGQ VAATTVTKAT
ETLAHKYIAG ENIKQALKTI ESLRRDKMAF TVDLLGEAVI TETEAQSYLE RYLDLMQQLT
AASKSWNKVG QIDEADGELI PKVQVSVKLT AFYSQFDPLD AIGSEEKVSS RIRVLLRRGK
ELGAAVHFDM EQYGYKDITF SILKKILLEE EFRDRTDIGM TVQAYLRDSE EDARGLIDWA
KQRGKPITIR LVKGAYWDQE TIKAEQRHWQ QPVYNDKAAT DVNFEKITQL LLENYQYVYA
AIGSHNVRSQ ARAIAIAESL QVPRRCFEMQ VLYGMGDKLG KALVDKGYRV RVYCPYGDLL
PGMAYLIRRL LENTANSSFL RQNLQNVAAE ELLVAPEVSL SRAKTQRREE EKGEKNYFVG
VADTDFAGDG ERKMAQEAFG LVRGQLGRMY LPLIDGEYVQ TQDVVESLNP SRFEEVVGKV
GLASVEQAEM AMQAAKNAFP GWRKTPVSQR AGILRKAAEL MELRRAELSA WIVLEVGKPV
READGEVSEA IDFCLYYAAE MERLNEGVSY DVAGEMNKYI YQGRGIAVVI SPWNFPLAIA
AGMTVAALVT GNCTILKPAE ASSVIAAKFA EILVEAGIPK GVFQYLPGKG SAVGAYMVNH
VNTHIIAFTG SQEVGCRIYA DAATLKMGQK HMKRVIAEMG GKNGIIIDES ADLDQAVVGA
VQSSFGYSGQ KCSACSRVIV VEAVYEEFVQ RFVEATKSLN IGEAELPSTQ VGPVIDDNAR
SRILEYIEKG KAESTLALEM SIPENGYYVP PTIFKDVPAD GIIAQQEIFG PVVAVIKAKN
FQKALEIANG TNFALTGGLY SRTPSHIEQA QADFEVGNLY INRTITGAIV ARQPFGGFKL
SGVGSKAGGP DYLLQFLEPK TVTENIQRQG FAPIEGAE
//
