ID A0A095Y4Z2_9ACTO Unreviewed; 1198 AA.
AC A0A095Y4Z2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=HMPREF1628_05260 {ECO:0000313|EMBL:KGF01712.1};
OS Actinomyces sp. S4-C9.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1219581 {ECO:0000313|EMBL:KGF01712.1, ECO:0000313|Proteomes:UP000035029};
RN [1] {ECO:0000313|EMBL:KGF01712.1, ECO:0000313|Proteomes:UP000035029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4-C9 {ECO:0000313|EMBL:KGF01712.1,
RC ECO:0000313|Proteomes:UP000035029};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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}.
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:KGF01712.1}.
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DR EMBL; JRMU01000010; KGF01712.1; -; Genomic_DNA.
DR RefSeq; WP_034508823.1; NZ_JRMU01000010.1.
DR AlphaFoldDB; A0A095Y4Z2; -.
DR eggNOG; COG0506; Bacteria.
DR eggNOG; COG1012; Bacteria.
DR Proteomes; UP000035029; 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 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:UP000035029}.
FT DOMAIN 132..422
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 524..942
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 723
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1,
FT ECO:0000256|PROSITE-ProRule:PRU10007"
FT ACT_SITE 757
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1198 AA; 131080 MW; 40DA616E3C52A075 CRC64;
MTAPEVTDFS QIAERALIRA RKWADESTKY PIDPAAKLLA DVLEDEGGLD YTVSFVDGVV
RPEDQQVAAD HLAETGKKNP DFLPWYLRTP ALIGGTVGKF VPEVSVPAAR RVFRQLVGDL
VVDVTNDKLG PAIQRLKAGG ASLNVNLLGE AVLGDKEAAK RLADTKRLLE RDDIDYVSLK
VSAVTGPHNP WGYDDVVDHA FTELLPLYRY AAAHPARKFI NLDMEEYRDL HLTIDVFKRL
LDQPEMKNYS AGIVLQAYLP DTLNAMKDLQ EWAAKRVENG GAPIKVRVVK GANLAMERVD
AAMRGWELTT WESKQATDAN YLRIINWAMT PEHLQNVKLG VAGHNLFTIA AAWELALERG
VQDQIEIEML SGMATQQASA VREDVGNLLL YVPVVSPDEY DVAISYLVRR LEENSADENF
MASIFDIGTD LGAFDKEKKR FLAAVEQMER EGDRRVGANR HQDRSTETAE DIAKPVTTPA
GGWTFKNTPD SDPSLPENLQ WARDIAARIK DSKLGNETIE AAVIDTEDAL NEMLDRAVEG
GREWAARSAK ERSDLLHKVG VELGKRRGEL IEVVASELGK SLQQADVEVS EAIDFAHYYA
ERALDLENLQ SAKFEPVDVT LVTPPWNFPI AIPAGGTIAA LAAGAAAILK PASIARRTGA
VLAECIWAAG VPETACILAS VGERQLGREL VTDKRVGRVV LTGGVETAQM FRSWDPTLRI
MAETSGKNAI VITPSADLDL AVKDVIDSAF GHAGQKCSAA SYVILVGSTG FSKRVRNQLV
DAAKSLHIGW GDDLSAEMGP LSSEPGEKLL AGLTTLDEGQ KWVLKPRRLD DTNRLWSPGV
RVGVEPGSEY HMVEYFGPIL GIMRVDTLEE AIAAQNMVDF GLTAGLHSLD PDEINYWLNN
VEAGNVYVNR GITGAIVQRQ PFGGWKRSAV GETTKAGGPN YLYGFGDIKP VEPTAEGERD
AAYPPAVEHE ANVKAPQLRE LLESAKRLLS EEDYARLAVA VESDQHAIDT EFGRLHDPSK
VGVERNILRY LPVGAQIRVG KYASLYEVFR AVSAGIALGE IVKVDPDDET SFIRELPAGA
YTGMDLTVST ETFLPTDPSI MLGNLGVDIL VENKRQFAER VQAEVEAGEN LDIRIRMIGE
DGDELRRAVD GSIDVAIWDG PVTTCGRVEI LPFVREQAVS ITNHRFGNKT PLSTQVLV
//
