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Database: UniProt
Entry: A0A177D7N3_ALTAL
LinkDB: A0A177D7N3_ALTAL
Original site: A0A177D7N3_ALTAL 
ID   A0A177D7N3_ALTAL        Unreviewed;       544 AA.
AC   A0A177D7N3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Homocysteine synthase {ECO:0000313|EMBL:RYN65486.1};
DE   SubName: Full=O-acetylhomoserine ami {ECO:0000313|EMBL:OAG15190.1};
GN   ORFNames=AA0117_g12140 {ECO:0000313|EMBL:RYN65486.1},
GN   CC77DRAFT_1080488 {ECO:0000313|EMBL:OAG15190.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG15190.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG15190.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG15190.1,
RC   ECO:0000313|Proteomes:UP000077248};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000291422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   bioRxiv 0:0-0(2019).
RN   [3] {ECO:0000313|EMBL:RYN65486.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN65486.1};
RA   Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA   Harrison R.J., Clarkson J.P.;
RT   "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT   species group including apple and Asian pear pathotypes.";
RL   J. ISSAAS 0:0-0(2019).
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; KV441495; OAG15190.1; -; Genomic_DNA.
DR   EMBL; PDXD01000065; RYN65486.1; -; Genomic_DNA.
DR   RefSeq; XP_018380611.1; XM_018529320.1.
DR   STRING; 5599.A0A177D7N3; -.
DR   GeneID; 29114914; -.
DR   KEGG; aalt:CC77DRAFT_1080488; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_1080488; -.
DR   OMA; IGNPRCS; -.
DR   OrthoDB; 6018at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   Proteomes; UP000291422; 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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU362118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   544 AA;  59885 MW;  5A374BA62BE4A141 CRC64;
     MAPFVEDENN VAATNGTSRP DSSTTNGTTS GTTNNQKIPD PNGITLSQLP ENHDPLQPYK
     IDKFDDGLRY DTLQIHGGHR PDKETHARAV PIYNSVSFVF TDSNHAKRIC STEEGGYFYS
     RISNPTVAVF EKRAAALEGG TAAIATSSGQ AAIFNTIICL AGAGDNIIAS INLYGGTYSL
     FKTLLPRLGI TVKWAKREIR EEFEQYIDDK TKMIFVETIG NPRCSIPDLQ DLGDLAHENN
     VPFVVDNTFG ACGTWCRPID FGANIIVHSA TKWMGGHGTT LGGVIIDCGT FDWGKAIHRF
     PRLSNKDGPM SFSYWKSFGN ICFAMAMRID ILMEVGSMLA PASAQQLLIG METLSIRCER
     HARNTMQVAR FLQAHPRIAW VNYPGLEGNI YHENAKRYLK NGFGGVLAFG PKGGEVASKM
     LMNYVKVVSH QTNVGDAKTL ATHPWNSTHV IMSEKDRREA GITPAFIRFS VGIEDVQDII
     DDLDQALAKL PEDLLNAFDE KLIQKLETHT KDEVLIGDLA DYNDTDVLVS KTNHPPGRQQ
     AVEN
//
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