ID B6QHT5_TALMQ Unreviewed; 442 AA.
AC B6QHT5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Homocysteine synthase CysD {ECO:0000313|EMBL:EEA22930.1};
GN ORFNames=PMAA_095340 {ECO:0000313|EMBL:EEA22930.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA22930.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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}.
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DR EMBL; DS995902; EEA22930.1; -; Genomic_DNA.
DR RefSeq; XP_002149097.1; XM_002149061.1.
DR AlphaFoldDB; B6QHT5; -.
DR STRING; 441960.B6QHT5; -.
DR VEuPathDB; FungiDB:PMAA_095340; -.
DR HOGENOM; CLU_018986_4_0_1; -.
DR OrthoDB; 6018at2759; -.
DR PhylomeDB; B6QHT5; -.
DR Proteomes; UP000001294; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; 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; IPR006235; OAc-hSer/O-AcSer_sulfhydrylase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01326; OAH_OAS_sulfhy; 1.
DR PANTHER; PTHR43797; HOMOCYSTEINE/CYSTEINE SYNTHASE; 1.
DR PANTHER; PTHR43797:SF2; HOMOCYSTEINE_CYSTEINE SYNTHASE; 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:UP000001294}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 442 AA; 47212 MW; 62B9AD66D20CCFC3 CRC64;
MAGQRFETLQ LHAGQEPDPA TNSRAVPIYA TTSYVFNDSA HGARLFGLKE FGNIYSRIMN
PTVDVFEKRI AALEGGVAAV AASSGQAAQF MAISALAHAG DNIVATSNLY GGTYNQLKVF
LPRLGIQTKF VNGDNAEDIA AAIDDHTKAV YVETIGNPRY NVPDFEAIAK VAHEKGVPLV
VDNTFGAGGY FARPIDHGAD IVVHSATKWI GGHGTTIGGV VVDSGKFDWG KHAARFPQFV
EPAEGYHGLK FWETFGPIAF AIRVRVEILR DLGSALNPFA AQQLLLGLET LSLRAERHAS
NALTLAKWLE KNENVSWVSY PGLESHASHE TAKKYLPRGF GGVLSFGVKG GAAAGSQVVD
GFKLISNLAN VGDSKTLAIH PWSTTHEQLS EEERIASGVT EDAIRISVGT EHIDDIIADF
EQSFQAASAA GADKTALPDR TA
//
