ID A0A364K9K7_9BACL Unreviewed; 378 AA.
AC A0A364K9K7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Methionine biosynthesis PLP-dependent protein {ECO:0000313|EMBL:RAL26981.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:RAL26981.1};
GN ORFNames=DL897_02780 {ECO:0000313|EMBL:RAL26981.1};
OS Thermoflavimicrobium daqui.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoflavimicrobium.
OX NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL26981.1, ECO:0000313|Proteomes:UP000251213};
RN [1] {ECO:0000313|EMBL:RAL26981.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26981.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Wang X., Zhou H.;
RT "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT Moutai-flavour Daqu.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAL26981.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL26981.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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:RAL26981.1}.
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DR EMBL; QJKK01000001; RAL26981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364K9K7; -.
DR OrthoDB; 9803887at2; -.
DR Proteomes; UP000251213; Unassembled WGS sequence.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:UniProt.
DR GO; GO:0003962; F:cystathionine gamma-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0102028; F:cystathionine gamma-synthase activity (acts on O-phosphohomoserine); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11808:SF92; CYSTATHIONINE GAMMA-SYNTHASE; 1.
DR PANTHER; PTHR11808; TRANS-SULFURATION ENZYME FAMILY MEMBER; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000251213};
KW Transferase {ECO:0000313|EMBL:RAL26981.1}.
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 378 AA; 41409 MW; 52E7F53553C3FD32 CRC64;
MKMNTKLIHG GVVADPQTGA VSVPIYQVST YQQASIGQHK GYEYSRTGNP TRTALEELIA
TLENGKRGLA FGSGMAAIST VLSMFNKGDH LVISDDVYGG TYRVLSQVFS RFGLEATFVD
TSEISYVMDA IRENTRAIYL ETPSNPLLKV SDIKLISEIC QAKNLYLIVD NTFMTPYWQN
PLDLGADIVL HSATKYLGGH SDVVAGLVVT KDEELGERIH FLQNSIGGVI GPFDAWLLIR
GMKTLGLRMR QHEESAGQIA RYLEQHPRVN KVYYPGLKSH PGHDLAKRQA RGFGGMISFD
VGSQAKAEKV LEQVNYFVLA ESLGAVESII SVPARMTHAS IPAETRAELG ITDGLIRISV
GIEDSEDLLD DLDQALTF
//
