ID A0A0U1LUE6_TALIS Unreviewed; 1654 AA.
AC A0A0U1LUE6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN ORFNames=PISL3812_04042 {ECO:0000313|EMBL:CRG87028.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG87028.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG87028.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG87028.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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 -!- 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 -!- SIMILARITY: Belongs to the oxoprolinase family.
CC {ECO:0000256|ARBA:ARBA00010403}.
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DR EMBL; CVMT01000003; CRG87028.1; -; Genomic_DNA.
DR STRING; 28573.A0A0U1LUE6; -.
DR OMA; VANSAMC; -.
DR OrthoDB; 674at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; IPR049517; ACX-like_C.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR008040; Hydant_A_N.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR003692; Hydantoinase_B.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR045079; Oxoprolinase_fam.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11365:SF2; 5-OXOPROLINASE; 1.
DR PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF19278; Hydant_A_C; 1.
DR Pfam; PF05378; Hydant_A_N; 1.
DR Pfam; PF01968; Hydantoinase_A; 1.
DR Pfam; PF02538; Hydantoinase_B; 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:UP000054383};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 35..349
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT DOMAIN 363..575
FT /note="Hydantoinase/oxoprolinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05378"
FT DOMAIN 595..889
FT /note="Hydantoinase A/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF01968"
FT DOMAIN 1019..1075
FT /note="Acetophenone carboxylase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19278"
FT DOMAIN 1094..1615
FT /note="Hydantoinase B/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF02538"
SQ SEQUENCE 1654 AA; 179149 MW; 51EBC77D1F8C3E63 CRC64;
MGSIAQASKF ENALFIPPDA IFEVTKRYLA DPNPNKVNLG QGTYRDGNGQ PWVLPSVRMA
KAKLGDGLHE YLPIEGLQDF RDEAVKIATC QALSGTGALL LAGLALRQAN SGIKTVYITE
PTWSNHELLF SRLGFEVKKL PYYKNGSFDS ASFIGTLEEA DSTCAVVLHA CAHNPTGYDP
TNEEWKNIAS VIKKNCILPI FDSAYLGFNS GSIDEDAWAI RYFTEDLELE ACICLSFAKN
MGLYGERVGL TAFVTSSSDQ ATIMSSILCN AQRATVSNPP AYGAKLAATV LGTPVIKKQW
YDDLVTMSSR IKSMRQMLYD ALVSLGTPGE WSHIIKQKGM FGYTGISEAQ VAYLEGMPVG
GIRIAIDRGG TFTDCVASVP GQDDILVKLL SVDPSNYQDA PVEAIRRVLE KATGRSYPKS
EKISLQGVES IKMGTTVATN ALLERKGEPT VFVVTQGMKD ILHIGNQSRP KLFDLRINKP
DVLYTEVVEI KERVTLEAWT ERKTPLNIDI DSDPALVKGN TGEVVRILQP LDVESTRKSL
QEVYDKGFRS IAICLLHSYT FPDHEQAVCG IAENIGFTHI SLSSKLSPTI RIVPRGNSST
ADAYLTPEIK RYIEGFERGF ENLGTSNCRC EFMQSDGGLV EFSGLSGLRA ILSGPAGGCV
GYARTAYVPD DKKAVIGFDM GGTSTDVSRF AGHLEQVFET TTAGITVQSP QLDINTVAAG
GGSILTWEAG MLQVGPESAS AHPGPACYRK GGPLTVTDAN LVLGRLRPEY FPNIFGPDED
LPLDIEASRK LFEEMSAKVN QHLPIKLTLE ELAAGFLDVA NEAMCRPIRT LTEAKGCDAS
LHNLASFGGA GGQHACEIAR KLGISRVLIH KYSSVLSAYG MALADVVHEE RSPCALLCTP
ENFSTFSKEL DRLQKESVKA LLQQRIRNEK ITSERYLNMR FHGSDTSMMI QETNGMDGFL
ASFKRAHQKQ FGFLPVGRDV IVDDLRVRSI GSSGVDVESP WKEELDTVSH FTLSATPETK
TKAIYFKETG WTQAPIYEIG SLRPGSCIAG PALIMDSSQT IVVTPKCSAT ILSNNIIIDV
EVLKKETISI THVDPIQLSI FGHRFMGVAE QMGRALQKTS VSTNIKERLD FSCTVFAADG
GLVANAPHVP AMIGSMAFAV KWQIDHWKDD LHPGDIILSN SPMCGGTHLP DLTVITPIFD
ENGEKIIFWT ASRGHHADIG GILPGSMPPN SKELWEEGAV IKSFKVVENG VFKEEELAEL
LMAPGKIDGC QGTRCLRDNI SDIKAQAAAN HRGSQLIHGL IEHYGLEPVQ FYMQKIIKTA
EVAVRDMLKN ISRMSGSKVL EAIDYMDDGT PIQLKVSIDE TTGDATFDFE GTGPEAYGNW
NAPIAICHSS IIFALRCMVN TEIPLNQGAI MPIKVIVPEN SLLRPTEEAA VCAGNVLTSQ
RIVDVIFKAF KAVAASQGCM NNLTFGTDDV EEAFGYYETI CGGAGGGPTW DGTSGVHTNM
TNTRITDPEV LERRYPVVLR QFCLREGSGG AGAHPGGDGI IRDIEFRIPI KVSILSERRA
FAPYGLEGGE DGKRGENIWI KAGGRSVNLG GKNTAMMGVG DRIIVKSPGG GGWGKASSIR
DGGFAPSVAK NVPKSFQAVA GGTVAMIESM GQSA
//
