ID A0A0A1SZS5_9HYPO Unreviewed; 648 AA.
AC A0A0A1SZS5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEJ90336.1};
GN ORFNames=VHEMI06127 {ECO:0000313|EMBL:CEJ90336.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ90336.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ90336.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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 -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; CDHN01000003; CEJ90336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1SZS5; -.
DR STRING; 1531966.A0A0A1SZS5; -.
DR HOGENOM; CLU_422838_0_0_1; -.
DR OrthoDB; 2255863at2759; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
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; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR11879:SF20; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF03328; HpcH_HpaI; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046}.
FT DOMAIN 29..399
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT DOMAIN 408..595
FT /note="HpcH/HpaI aldolase/citrate lyase"
FT /evidence="ECO:0000259|Pfam:PF03328"
SQ SEQUENCE 648 AA; 70640 MW; 02D9B7388382FB00 CRC64;
MSLFDQVPTL PPDNGFALLE AFRADPFEKK VNLCPGIYQD ESGQTWTLPS VKKARETLLG
NPDLKHDISP LTGHPAFVSA ARRIAFQDAL ESRHVTSMQT IAGTGANHII AQLLSDVATP
KTVWLSDPSW ENHTKIWSHV NSKIEQRFYP YYNTETFALN DERILATLQE HAKKGDVVVL
QACAHNPTGV DPSQEFWKKM AKLCHEKDIF PVFDLAYQGF ATGDVLNDGW AIRYFAGYAG
GDIEFAVAQS FSKTFGLYGE RTGALHVVTR SEETANKVVG ALKKICRAEL TSTPGFGAKI
VGTIMQDKEL ETQWYQDLKT MSDRLQDMRK KLYDQLTKRN TPGNWAHFLS DIGMFSMTGL
SPTQLATLQD EYHIYMLPMG RLSFTGLTSS NVEYVAAAIH TAFGIKLSAN PAVIQIAANS
GFDALFIDLE HSTLSIDDAS QLCWSGLQGG ITPFVRVPGE CGSGLVQRVL DGGAMGIIFP
HMSSPEQAKE AVSICKYPPM GRRSMTGQLP VFGYKANAAQ TVIRHSNDSA SSVIVMIESK
KGVDCAAEIA AVEGVDTLLV GSNDLAIELG VPGDFESTEF RSALETISEA CKKNNKIMGL
AGIYNQPNFH DWAVAKLGVR FILGQLDVGL IAAGAVQCFA ALPVAKLP
//