ID A0A3E2HHP4_SCYLI Unreviewed; 880 AA.
AC A0A3E2HHP4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
DE Flags: Fragment;
GN ORFNames=B7463_g3458 {ECO:0000313|EMBL:RFU32887.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU32887.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU32887.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU32887.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000256|RuleBase:RU000480};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU000480}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:RFU32887.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NCSJ02000046; RFU32887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HHP4; -.
DR STRING; 5539.A0A3E2HHP4; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR019529; Syntaxin-18_N.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF55; GLUTAMATE OXALOACETATE TRANSAMINASE 1, ISOFORM B; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF10496; Syntaxin-18_N; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 2..95
FT /note="SNARE-complex protein Syntaxin-18 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10496"
FT DOMAIN 496..866
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 310..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU32887.1"
FT NON_TER 880
FT /evidence="ECO:0000313|EMBL:RFU32887.1"
SQ SEQUENCE 880 AA; 96555 MW; 1E67E5C1A39E4F0B CRC64;
MTDLTPILND LLKKHNAGPT ANPALTLQSI DGFLKEAYRI NSHISSLNTY LRSIRQSYLS
TTPPPRRTTT QYSLKPNASS NRQWKYLTDQ QRDEIDAETK QLLRELNVSI RNLADAEQLR
QDTESTLRRK KYHRLGLGAL GAWAAGGGGG ANGGRQTRSR EEEEEVVRSD AIKLHRESVL
WFLRRMLQGA GQVQAEMMEK RILREMEKNK SVLARTRRAS ISEFGGFERV GSVAGVGGGG
GGMKGPAGGG AGLTAVEMET RELYPEEQLS EEQIQMFEKE NQEMLKHYES TLDQVRLFQD
GGKVADRDLG ATDATGQQPG DAIGAHRPAG GGFVPHDGEC RRWEQAAEEG RGEEEHGQVP
SHTEQYTRVR DGTGPLGKEE SERWKEKMHA TAAPKEKLTM ARFDASTSHH SLATAASSST
PTSSISSATF PSASSSFSSS SPSTSSSSPQ ARLQSIAAHM SSSSNTSFSP EAVPQAPEDP
LFGLMAAYRA DSFDRKVDLG IGAYRDDNAK PWVLPVVKKA DDILRTDPNL NHEYLPIAGL
PDFTKAAAKL ILGADSPAIQ ESRATSVQTI SGTGAVHLGA LFLQKFYPGS PAVYFSNPTW
ANHNQIFTNV GLPIATYPYF SKSTKGLDFE GMKKGIADAP NRSIILLHAC AHNPTGVDPT
QEQWKELATL IREKSHFPFF DCAYQGFASG DLARDAWAVR YFVEQGFELC VAQSFAKNFG
LYGERAGCFH FVTSPAPDAA NTIKRISSQL AILQRSEISN PPAYGARIAS LVLNSPELFT
EWEQNLLTMS GRIISMRKAL RGKLEELGTP GKWEHITDQI GMFSFTGLNE KQVAKLREEA
HVYMTKNGRI SMAGLNTKNV EYFAHAVDKV VRETEADSKL
//
