ID Q021Y6_SOLUE Unreviewed; 391 AA.
AC Q021Y6;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Cystathionine gamma-synthase {ECO:0000313|EMBL:ABJ84227.1};
DE EC=2.5.1.48 {ECO:0000313|EMBL:ABJ84227.1};
GN OrderedLocusNames=Acid_3250 {ECO:0000313|EMBL:ABJ84227.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ84227.1};
RN [1] {ECO:0000313|EMBL:ABJ84227.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ84227.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) 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|RuleBase:RU362118}.
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DR EMBL; CP000473; ABJ84227.1; -; Genomic_DNA.
DR AlphaFoldDB; Q021Y6; -.
DR STRING; 234267.Acid_3250; -.
DR KEGG; sus:Acid_3250; -.
DR eggNOG; COG0626; Bacteria.
DR HOGENOM; CLU_018986_2_0_0; -.
DR InParanoid; Q021Y6; -.
DR OrthoDB; 9803887at2; -.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Transferase {ECO:0000313|EMBL:ABJ84227.1}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 391 AA; 42685 MW; 1F80333A04D91B6C CRC64;
MKIHTQAVHT GDRRKPGAHT PVTTPIHLAT SYFYDSMEQL DRVFADQEKG YCYARHDNPS
TGALEELMCV LEAGDAALAC ASGMAALHTA IAAALTDRRR SIVAASAMYG ATVGLLMNVF
EPAGVSVRFA DVCDLEGLRK VVAEAQPGCI VMETISNPLL RVGEIDRIAE IAREAGAALV
VDHTFATPLL ARPLELGAHF SVHSVTKYLA GHGDVLGGVV VTNKDHAEIL RALGRTIGPV
LGPFESYLTM RGIKTFPLRM ERQCANACRV ASWLAAHPRV ERVFFTGDPQ HPDAAAIRRL
FPEGLYGAMM SFEIRDAGRE EIFRFMDALK MIVRATSLGD VHTMMLYPVM SSHRELSPKH
RLRMGIRDNL VRLSTGIEAA EDIIADLEQA L
//
