ID F8L492_SIMNZ Unreviewed; 1206 AA.
AC F8L492;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:CCB90139.1};
GN OrderedLocusNames=SNE_A22620 {ECO:0000313|EMBL:CCB90139.1};
OS Simkania negevensis (strain ATCC VR-1471 / Z).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Simkaniaceae;
OC Simkania.
OX NCBI_TaxID=331113 {ECO:0000313|EMBL:CCB90139.1, ECO:0000313|Proteomes:UP000000496};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S.A., Horn M.;
RT "Unity in variety -- the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 0:0-0(2011).
RN [2] {ECO:0000313|EMBL:CCB90139.1, ECO:0000313|Proteomes:UP000000496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1471 / Z {ECO:0000313|Proteomes:UP000000496};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
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; FR872582; CCB90139.1; -; Genomic_DNA.
DR RefSeq; WP_013944605.1; NC_015713.1.
DR AlphaFoldDB; F8L492; -.
DR STRING; 331113.SNE_A22620; -.
DR KEGG; sng:SNE_A22620; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005682_2_0_0; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000000496; Chromosome gsn.131.
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; cd07125; ALDH_PutA-P5CDH; 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 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:UP000000496}.
FT DOMAIN 153..451
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 556..993
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 769
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 803
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1206 AA; 136776 MW; 48BF6EAC259DEF5F CRC64;
MQEASESKHL KAAREMLSAA YHTPLTLKER QEKAIELASH ILLESNQIIT KDDQKKHEEL
SRMMRDPVGK VFTTAMTDQC FRSHDYKRIA NQMIYLLNLY GIPKFLSSFK RLQLYLFKLL
GDKFANILVP MAMRQLRKET SKVIIPGEKG PLAKHIKKRK AQGIRLNLNH LGEAILGEEE
AKKRLEVYLR DLKNPYIDYV SIKISTIYSQ LNLLSYENTL DNLAARLREL YRAAIENKTQ
LKDGCTSHKF VNLDMEEYRD LHLTKDLFIK VLSEPEFHSL SAGIVLQAYL PDSHDIQKEL
THWAMDRVRN GGAPIKIRIV KGANMAMEQV EASLRDWEQA PYEHKIQTDA NYKSMILYAC
EPEHSKAVHI GVASHNLFDI AFAMLLRLEN RVEQEVTFEM LEGMADHTRQ VVQALTNDIL
LYCAVATKED FQSAIAYLIR RLDENTGIEN YLAHSFGLTP ESKEWSIQCS LFRDACQMIP
TIYQTPRRTQ NRFDPPSHLD IKALFENESD TDFSLAENRK WGKAILDTWK NKQIDPIPLV
IEGKEISHSD PEGKGYDPST PSRPLYTYSM ASWEEVDQAL RCAKNYEKTW GKTSVEERCK
LLSKVAQRLR ETRADLIGAM VADGGKLIME ADVEHSETID FAEYYLRSMQ HLNGLSDIQW
SPKGTILVTP PWNFPTSIPG GGICTALVTG NCVLFKPAPE AVLAGWELVK AFWDAGIPKE
ALQFINCADD PVGSQLIKDT RVNSVILTGA TSTAHLFAKM RPGIDLSAET GGKNALIISS
LSDRDLAIKD LVQSAFGHNG QKCSAASLAI LEKEVYDDPH FRKQLRDAAA SLKVGSAWDL
SSKITPLIRE PGDDLKKGLT TLEEGEFWLL EPKQDSSNPN LWSPGIKFGV HKGSYTQQTE
FFGPVLGVMR AENIDHAIHL ANSTPYGLTS GIHSLDKREI KKWQNLIIAG NCYINRTITG
AIVRRQPFGG CKNSSYGHGS KAGGPNYLTQ FMHATQKGIP KEKFPVGEWV NNLTRFLEKF
DLSAEELGMW YASVSSYAFF WQQFKRDKDS SKIVGQDNFF RYLPQKKLIF RIGPNTKPMD
YLRVFAAALT CETRLEVSWE KSRDAKVRQA NWEALLPIFN IVEEDQATFI KRMCSCHFKR
IRMLEEPSAE MKQAAAASAT YIDHTPVLAN GRIELLHYLR EMSLSVDYHR YGNLGLREGE
LRKPIL
//
