ID A9FN92_SORC5 Unreviewed; 480 AA.
AC A9FN92;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN OrderedLocusNames=sce8233 {ECO:0000313|EMBL:CAN98403.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN98403.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN98403.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; AM746676; CAN98403.1; -; Genomic_DNA.
DR AlphaFoldDB; A9FN92; -.
DR STRING; 448385.sce8233; -.
DR KEGG; scl:sce8233; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_517569_0_0_7; -.
DR Proteomes; UP000002139; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT DOMAIN 88..456
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 480 AA; 53394 MW; F040589B0C8E23C7 CRC64;
MLDVYARAKN PDDPIELRDL WLGRVEHELG RHAHRPSLAE RWRAATLRRQ VHPSEVLTSR
ATVRFIKELF NWFFRDDLYG ELRSDDHIIL SSGSVDEQAW GLPEALKDCV RFALERDWYG
YSDSCGRRPA REAVAMYENA RIDGAVYTAD NVALTMGGTF AISALADFIL SGAPREGAPV
LCGIPNYPPL VESIARRRNV ELVPLPSRAG HTSLEPLIAA LTPRTPLVLL QTVANPTGAA
VSDADLGRLI NAASPSTMIV LDECHEWLGP LGRCSQRRAA TNVIRVFSAS KTWSAPGLKI
GWFLADAGFM ADYYEYASTT FGGPPSFFYT LVEVLARMER WLITGVTEPG AAEVDEFERS
YGLDRAQLST AYDRYRTERR ARQDALQTLR DASIGGLARA SARVISPRCS INLAFELPGW
NDSYRCFRDL LRQSRVAVFP GILTFCFSGG IVRVTTARQW HDLSSAIARL EAQLGLPRGR
//
