ID A0A0V0TTQ0_9BILA Unreviewed; 1865 AA.
AC A0A0V0TTQ0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
DE Flags: Fragment;
GN Name=T01C8.5 {ECO:0000313|EMBL:KRX42410.1};
GN ORFNames=T05_184 {ECO:0000313|EMBL:KRX42410.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX42410.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX42410.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX42410.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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 -!- 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:KRX42410.1}.
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DR EMBL; JYDJ01000145; KRX42410.1; -; Genomic_DNA.
DR Proteomes; UP000055048; 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 CDD; cd16448; RING-H2; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR002083; MATH/TRAF_dom.
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; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF00917; MATH; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SMART; SM00061; MATH; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480,
KW ECO:0000313|EMBL:KRX42410.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}; Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Transferase {ECO:0000256|RuleBase:RU000480, ECO:0000313|EMBL:KRX42410.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 495..609
FT /note="MATH"
FT /evidence="ECO:0000259|PROSITE:PS50144"
FT DOMAIN 1787..1828
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 763..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1150..1339
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 786..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1865
FT /evidence="ECO:0000313|EMBL:KRX42410.1"
SQ SEQUENCE 1865 AA; 209265 MW; 1E0E7D317171372D CRC64;
MSLFSFVNPA PPVEVFHINQ CFQSDPNPKK VNLTIGAYRT EEGKFWVLPV VAKAESILIN
SPTHNHEYLP MLGNNKFSSL AIKLLFGEHT EKLEKKLLCA QSLGGTGSIR AGLEFLNRTC
GLKEAYISDP TWENHRLILE YCGYSKINTY RYWQNEKRAV DFEGMLQDLQ AAPEKSVVIL
HGCAHNPTGM DLSKQQWIEL FELLQKKQLF PFFDLAYQGF ASGDPDSDAW AVRYFASRGI
EMCVAQSFSK NFGLYNERVG NLVVVFNDEK VLASCKSQLS LVVRANWSNP PNHGAKIVET
VLSDPELTNQ WLENVRVMST RIQCMRKALR AKLEELKAPG TWNHITEQIG MFSYTGLSEK
QVKYLAEAYH IYMLKSGRIN MCGLNPQNID YVASALPKAN NVEGEEEEEK PCCVKSPCDC
CDAEESELTV KPPKRCCQLF NKLLSSNHTS TVACQTESLD WGVAVKKTGI ESGGELASNS
PVSSVKKEEE NVVAEGLLRL MIHNFRHMTD TVRGPAKIIN GVPWKIMVMP RQHVVAKKGT
QNSWSCQAAA ELKIKALKSH ASDFVRKTNH NYSVKENDWG YSCFMTWADV MDESQGYLKD
ECIQLEVIVR AETPKGILTH EAFVKKIQDY IRLADLQRSR GLVDKAIEVN QTAARFCKDK
DTDMKEELDK QRLKLIEEKL KESISRIEKN KDYEGSVDQA AALETLRQAI TGSIVFSEMT
GSETDSPKSG SAEERVAANL CGSQLHFQDT VLKMVKEKYS QWDRPVKQSS DESVSDGAKN
PIIENGAKEN KSKNEVGYCS KEKQSRTVAS QSSGAANSVD NNQSEQRRKQ KQNPQQQKQQ
QQQQQQQQQQ QKQQQQQQQQ QKQKQQQQQQ QQQQQQQHRA TPAKGDKTPT VVPPAATPPS
SGGASQQAPW IGNYGRDSCS LPVNLADQSA GTAMMTTWRT SMVNGEATTT TATFTKNENG
TMILSNETRN DLSSIKGTLQ RLASLARDGV EVANTVQSNL SKVAFRLTAP EFLPDLAGAK
AQAGNKQQQP GCSGKTASAT NRRMSQKQHQ QQQHVCTSDD QSSKGGKKHQ HQHQHQQQQL
HKCPNCAAEK AAAFYSAVQS SDSLSELDTL SLQLQLRGAD VRERNVPELL SKFKFFANSN
TETYRICDMI KKCEKKLKEY EKATSASKKE LNEAAERYLV NEQKLVKEVE TLKTQLDQAK
ERFEKQVALS KEHRKEFRKL EKRLRNECMS PSTKAELMTK AENLENELKK LKTKNEEERQ
RNSEEIRKHV EQFKVAQREA HSLGLENDRL QLDVDSKSQM IEKMEKEREK EVLQMQTTLK
EVMDRAKRHE IEILELRLQM GLKALQGSLD DCQRHLNQFD EIAKKHGQVI CHEEMKVFLA
CQQEWIKTKE TVKEMMQKLK VDDFRHQIEL VRGGTLLQSL MPIEIPKPPA PPPFPRFCYS
IQQQQQQPQQ QQQPMPPIGQ QMSSAASVRG GGGGQQQKQS MGIYSTNNGT LRGANTAAAA
SLSGSGADMH FSSGFGGMAK IGNSSSSIYG TNQQSVVEQQ QHRSGGGGGG SGTAASSSDF
SPWADGTQSY FNGKAFGTMF DSFSSSSSTV ASGPTMPPNQ QQPSPLPLHH HHQQQQQQQQ
QQQQQQQVGA AGTIGQWSNW SKYQQRPPSA LSSLQTSSTP DYSSVKQQRP PSAVQRSASP
GMTMSTSDCN QIFSSEGVDW DFLCDYFDSR CPTVQSEQIR EALSEFRYNH FEKFKTLPTM
SLWATLLKFM VAKLKLPPPP PPPSLTSGFG KADNFVGSRR SAAEEFCMIC HALLRPEDHC
TTLSCSHKFH KNCINQWMAE KHACPSCSSF ALPPEEYPDL AFVCFLHPFY PVQQECRFSI
ALVEE
//
