ID B2ULM2_AKKM8 Unreviewed; 388 AA.
AC B2ULM2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Amuc_1589 {ECO:0000313|EMBL:ACD05409.1};
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741 {ECO:0000313|EMBL:ACD05409.1, ECO:0000313|Proteomes:UP000001031};
RN [1] {ECO:0000313|Proteomes:UP000001031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013
RC / CIP 107961 / Muc {ECO:0000313|Proteomes:UP000001031};
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP001071; ACD05409.1; -; Genomic_DNA.
DR AlphaFoldDB; B2ULM2; -.
DR STRING; 349741.Amuc_1589; -.
DR PaxDb; 349741-Amuc_1589; -.
DR KEGG; amu:Amuc_1589; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_0; -.
DR OrthoDB; 9813612at2; -.
DR BioCyc; AMUC349741:G1GBX-1695-MONOMER; -.
DR Proteomes; UP000001031; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; 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 PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
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:RU000481,
KW ECO:0000313|EMBL:ACD05409.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001031};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ACD05409.1}.
FT DOMAIN 32..381
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 388 AA; 42441 MW; 6A744B6DB3647B73 CRC64;
MDMISPSIAA LTPSLTLKVT NRAKAMKASG EEVYGLAGGE PEMDTPENIK QAAIAALNNG
ATKYTPSAGL PALRQAIAEK LKRENNLEYD FTQITVGAGA KHACFNAIMA TVSEGDEVII
PAPYWVSYPE MVRMCGGIPV IVETTAENGW KLTAEQFEEA MTPRTKMVIL TTPNNPTGSV
YSEEELRALG EVALSEDILI LADEIYEHLV YGDARHVSIA SLSPELYDLT ITINGFSKGY
AMTGWRLGYS AAPAAIAKAI QMIQDHTTSN VCTFAQYGGI EALTGDQSFI SDMRDEYDMR
RQYVYSRLSA IPNISVVEPQ GAFYFFVDTS RLGLTSLNLC DKLLERYKVA AVPGIAFGND
KAIRISYCTT LDILKEALDR FEEFCKAH
//
