ID A0L8H0_MAGMM Unreviewed; 421 AA.
AC A0L8H0;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Mmc1_1755 {ECO:0000313|EMBL:ABK44263.1};
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK44263.1, ECO:0000313|Proteomes:UP000002586};
RN [1] {ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
RN [2] {ECO:0000313|EMBL:ABK44263.1, ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=22581902;
RA Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA Bowser S.S., Dean A.J., Beveridge T.J.;
RT "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
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|RuleBase:RU000481}.
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DR EMBL; CP000471; ABK44263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0L8H0; -.
DR STRING; 156889.Mmc1_1755; -.
DR KEGG; mgm:Mmc1_1755; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_5_5; -.
DR Proteomes; UP000002586; 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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42832:SF1; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAC; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
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:ABK44263.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ABK44263.1}.
FT DOMAIN 55..394
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 421 AA; 47190 MW; E4181E39E80E42FA CRC64;
MTETAPFMGV GWLCRLSSCM NGPSMEEFHR IKRLPPYVFA VVNELKYKAR NRGEDIIDFG
MGNPDQPTPK HITDKLIEAV QDGRNHRYSL SRGIGGLRRA VCAYYKRRFG VDLDPESEAI
VTIGSKEGLS SLAMAITEPG MNVIVPSPTY PIHEYSFLIA GAHIQRVKIS RDNDFIEDMK
VAVRNHWPRA QVLVVNFPSN PTAQVVELDF YQKVIDFAKE HNIWVISDVA YAEICFDGYK
APSILQIPGA KDIAVEFYSL SKTYNMPGWR VGFCVGNPHL IKALSRIKSY LDYGMFQPIQ
IAATVALNGP QDCVAEINEI YRQRRNVLID GLARAGWAIE RPKASMFVWA EIPDEFKAMG
SLEFSKLLLK EAKVAVSPGV GFGVYGDDHV RIALIENEHR TRQALRSMRR FLSAGSDVAG
D
//