ID   C7LY42_ACIFD            Unreviewed;       421 AA.
AC   C7LY42;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACU53650.1};
GN   OrderedLocusNames=Afer_0700 {ECO:0000313|EMBL:ACU53650.1};
OS   Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS   ICP).
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidimicrobium.
OX   NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU53650.1, ECO:0000313|Proteomes:UP000000771};
RN   [1] {ECO:0000313|EMBL:ACU53650.1, ECO:0000313|Proteomes:UP000000771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC   {ECO:0000313|Proteomes:UP000000771};
RX   PubMed=21304635; DOI=10.4056/sigs.1463;
RA   Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT   (ICP).";
RL   Stand. Genomic Sci. 1:38-45(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001631; ACU53650.1; -; Genomic_DNA.
DR   RefSeq; WP_015798139.1; NC_013124.1.
DR   AlphaFoldDB; C7LY42; -.
DR   STRING; 525909.Afer_0700; -.
DR   GeneID; 80814806; -.
DR   KEGG; afo:Afer_0700; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000000771; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACU53650.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000771};
KW   Transferase {ECO:0000313|EMBL:ACU53650.1}.
SQ   SEQUENCE   421 AA;  44675 MW;  F58D7F552722796F CRC64;
     MGRLAPVWSK VSPITVTHGR GARVWDTNGQ AWLDMTAGIA VTSTGHAHPK VAEAIARQAE
     RFIHAQVNIY THDLLQPLAD ALDAITPDGI DTFFFSNSGA EATEAAVKLA RQATKRPNVI
     VFQGSFHGRT AQAMAMTTSR TGYRAGYMPL PAGVFVSLFP GFPRSSRVGD EVSVDEALDY
     LDYLLASQTA PAETAAVVIE PVLGEGGYIP APAAFLTGVV ERARAHGIVF VADEVQTGFG
     RTGRMFAVEH ANVTPDILVM AKGIASGFPF SGIGASWELM ERWPVGSHGG TYGGNPMGVA
     AALATIQVIQ EEGLVDNAAR RGAQLQASME RIAEKFECVS RVRGLGLMVG VELRDDAGRP
     DADLVGRVLA EMQASHRVLA MSAGTFGNII RWMPPLVVSE AEIDEAAAAF EASLAHVLAQ
     R
//