ID C5ZXR5_9HELI Unreviewed; 1159 AA.
AC C5ZXR5;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN Name=putA {ECO:0000313|EMBL:EES89933.1};
GN ORFNames=HCAN_1224 {ECO:0000313|EMBL:EES89933.1};
OS Helicobacter canadensis MIT 98-5491.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=537970 {ECO:0000313|EMBL:EES89933.1, ECO:0000313|Proteomes:UP000007032};
RN [1] {ECO:0000313|EMBL:EES89933.1, ECO:0000313|Proteomes:UP000007032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13241 {ECO:0000313|Proteomes:UP000007032};
RX PubMed=19542273; DOI=10.1128/JB.00729-09;
RA Loman N.J., Snyder L.A., Linton J.D., Langdon R., Lawson A.J.,
RA Weinstock G.M., Wren B.W., Pallen M.J.;
RT "Genome sequence of the emerging pathogen Helicobacter canadensis.";
RL J. Bacteriol. 191:5566-5567(2009).
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; CM000776; EES89933.1; -; Genomic_DNA.
DR AlphaFoldDB; C5ZXR5; -.
DR STRING; 537970.HCAN_1224; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005682_2_0_7; -.
DR UniPathway; UPA00261; UER00373.
DR Proteomes; UP000007032; Chromosome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004657; F:proline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
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 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 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:UP000007032}.
FT DOMAIN 133..420
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 517..961
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 736
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 770
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1159 AA; 132614 MW; 2D76F37176FCBAD9 CRC64;
MKQIIEESLK FAEELQSKIE ANISQSEREF HGKMQKLLSN PKNKVMLIEL LDRSFRCKDK
RASFELIEHT LNKFGIADFF SPFEKFLLYS FITLGRFAPN VSVPFFVSHL RKDTSAMVLD
ANESFLKPHM EKRKQNDHIT LNVNLIGEEV LGEAESQYRI QKYEEALQSS FITYISIKIT
TIFSQINIID FEYSKNEVVK RLDHLYALAE VEEKRQGVEK FINLDMEEFR DLELTVAAFM
ESLSKFNIKA GIVLQAYIPD SYEYLKKLFA FSKQRVQEGK KPIKIRFVKG ANMESEETIA
SQRGWELPTF SKKIDTDSNY NKMLDFILQD ENYKYINIGI ASHNIFEIAY AYTRIKEANA
FGSFTFEMLE GMSLQCSYEI SKLHNLILYA PVCDEAHFNN AIAYLVRRLD ENTSEDNFMR
YFFNLKVGDA NWQAQKALFL KSLEGIKNLD NSTHRTQDRN KELTIKSAYE TKVFKNESDT
DFILPQNREW AKKIKEKYEN LEAYEVYPVI SEVIKKADLK HIEVRDKIKN RLIAQVHLAG
EKEIKQALEV AKNSKFKEKS FDEIHQILAK AAKIMREKRG DLIGIAALEV GKTFLEIDPE
VSEAIDFTEF YPHSLATLIK QNPKTKFAPK GVGVTIAPWN FPVGISVGTI VAPLAAGNAV
IYKPSSLSTL TGYMICECLW EAGVPKDALI FLPSKGSDIS KYLLTNEAIK FAILTGGEET
AYRMLEANPT LLLSAETGGK NATIVSKFAD RDSAIKNIIH SAFSNSGQKC SATSLLVLED
EVYNDKEFKK TLVDAASSML VGSPFEFKNK IAALCDEIDP KVQRALDELK PYEEWALKPK
FIDDNKHLMS PGIKYGTKKG DFTHMTELFA PILSVMRAKD LKEAIEIVNA TGYGLTAGFE
SLDEREWEYF HTHIEAGNIY INKPTTGAIV LRQPFGGVKK SAIGFGRKVG IYNYITQFLE
ITQEEADNHL LENRISTTLK DLGMSELDKM AQSYAYHYKN EFSVAKDYVD IRGEDNLFSY
TKIKNLAYRV CKEDSLRDIL GVILAANIAT IELLVSFEEN PHIQKAKELC QKLGFKVEFL
EETQEDFVNK ISNYERIRYH LIPNVDDKIY REASRLAKII IREKPLINGR FELLFYHNEK
SVSISYHRYG NLGIRALEK
//
