ID A0A2A3ACK8_9MICC Unreviewed; 1204 AA.
AC A0A2A3ACK8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
GN ORFNames=CKW39_13690 {ECO:0000313|EMBL:PBB07405.1};
OS Kocuria sp. WRN011.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=2029858 {ECO:0000313|EMBL:PBB07405.1, ECO:0000313|Proteomes:UP000218573};
RN [1] {ECO:0000313|EMBL:PBB07405.1, ECO:0000313|Proteomes:UP000218573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRN011 {ECO:0000313|EMBL:PBB07405.1,
RC ECO:0000313|Proteomes:UP000218573};
RA Zhang G., Wu G.;
RT "Kocuria alkalisoli sp. nov., isolated from saline alkaline soil.";
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:PBB07405.1}.
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DR EMBL; NSGI01000011; PBB07405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3ACK8; -.
DR OrthoDB; 9812625at2; -.
DR Proteomes; UP000218573; 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; 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218573}.
FT DOMAIN 138..430
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT DOMAIN 538..953
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 453..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 734
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
FT ACT_SITE 768
FT /evidence="ECO:0000256|PIRSR:PIRSR000197-1"
SQ SEQUENCE 1204 AA; 131990 MW; F260674915BAE5C2 CRC64;
MTSNITVLTN PRELADASVD LVRQWLDRAQ DNKKRSSQKN PAEDRLSTVL QDPHGLEFTV
GFVDRVIRTE DTKAAAKALQ DIAKLTPESM SAVDRAQIKA GTALSDKLSS IVVPAARTRL
RQMVGHMVVD ARPGPFGKSV KAMKEKGHRL NINLLGEEVL GEHEAKKHLN DAKELLHRPD
VDYVSLKVSS VVPQLSHWGF DRTADRVVER LLPLYEAAAS KETGTMFINL DMEIYSDLEL
TMEVFQRLLN KPQLKNLEAG IVVQAYLPDA LGAVKRLSEW SAERVADGGA EIKVRLVKGA
NLALERVDAE MHGWPIATMP SKQATDTNYK RVLSWLFTPE RMRGLKLGVA GHNLFDIALA
HLLADKRGVT DRIDFEMLQG MATEQSEAVS TDVGQLLLYV PAVRPTEFDV AVSYLVRRLE
ENSASANFMS GIFDLAPDNR IFKREESRFR AALEDLEPDP EPLSPSRTQD RAQETAGDEP
TQPLDEPFMN EPDTDISTRA NQEWAEKIAA HIADKEWFEN LPVPEVLKDV EDDSSEAVEA
VNDVVARAKA AGKTWADTPA RERAEILNRA GDILAARRGH LLAVAGAETG KVLEQGDPEI
SEAVDFCRYY ARRALELEFV DGGKFTPHHV TVVTPPWNFP IAIPTGTTVA PLATGSAVIH
KPSPETRRCS AAICEALWEA GVPRDVLQLV DAVEGDAGKA LISHPDVQRV VLTGAYETAQ
LFAKWFPERP LTAETSGKNS LVITPSSDRD QAVWDLVSSA FGHAGQKCSA ASLGILVGSV
ATSDRFRRQL IDAASSMVVA WPDDLQASVG PTVEKPEGKL LKALTELEPG EEWLIEPEQL
DDSGKLWRPG IRTGVKPGSF FHLTECFGPV LGLMRADDLD EAIELQNATD YGLTAGIHSL
DADEILHWVD RVQAGNLYVN RGITGAIVQR QPFGGWKRSS VGLGAKAGGP NYLTSLGRWC
REDFTSSGSD RSAAGAWVLE PRVHRGLDAV LPLVGEDDQV WLRRAAMSDQ SEWQREFGQV
KDPTALVSEA NLFRYRPRTV IVRAAEGASL TDILRVGLAA SRSGSEVILS PAEELPEQVG
RLFTTVLSPA SDVDFAHALG AGSLGAFAEL SDREILNDTA LNVDHGARVR VIQPWDGTDD
DLKPLYEVRA EHPDIALITD DVVGTGRIEL MYMLSEQAVS ITMHRFGNHS PSMDRVVTEI
RANK
//
