ID I3IAX4_9GAMM Unreviewed; 326 AA.
AC I3IAX4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=N-(2-amino-2-carboxyethyl)-L-glutamate synthase {ECO:0000256|ARBA:ARBA00016985};
DE EC=2.5.1.140 {ECO:0000256|ARBA:ARBA00012331};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN ORFNames=O59_001887 {ECO:0000313|EMBL:EIK45209.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK45209.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK45209.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK45209.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000256|ARBA:ARBA00000298};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. SbnA subfamily. {ECO:0000256|ARBA:ARBA00008519}.
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:EIK45209.1}.
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DR EMBL; AICM01000003; EIK45209.1; -; Genomic_DNA.
DR AlphaFoldDB; I3IAX4; -.
DR STRING; 1134474.O59_001887; -.
DR PATRIC; fig|1134474.3.peg.1732; -.
DR eggNOG; COG0031; Bacteria.
DR HOGENOM; CLU_021018_1_0_6; -.
DR Proteomes; UP000003395; Unassembled WGS sequence.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR023927; SbnA.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR03945; PLP_SbnA_fam; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF254; N-(2-AMINO-2-CARBOXYETHYL)-L-GLUTAMATE SYNTHASE; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 9..278
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 326 AA; 35931 MW; E627FFECA120642A CRC64;
MNCIFGNQDV RVYAKLELLN PGGSVKDRPA KFIIEQGLRD GSIPKGAHLI ESTSGNLGVA
LAMMSRVHHL QLTCVVDPNI SKTNLEIMRL YGAHIEMVTE RDACGGYLET RIARVKSLLQ
EKQNGVWINQ YANVRNWQSH YHGEGEELLK QLPERPDYLV MGVSTSGTIL GIARRLREAY
PELKVIGVDA LGSMLFGNKP GKRFLPGIGA SRVPELLAKE EIDDVIYASD LESCESCLDL
VKDEGIFAGG SSGSVVAAIK KLIPHIPKGS CIATLFPDRG DRYMDMVYNA EWRATLQQGD
AQFIPQFIRK KTPAVCTPEY DVSLAV
//
