ID C7M1J8_ACIFD Unreviewed; 458 AA.
AC C7M1J8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ACU53047.1};
GN OrderedLocusNames=Afer_0076 {ECO:0000313|EMBL:ACU53047.1};
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:ACU53047.1, ECO:0000313|Proteomes:UP000000771};
RN [1] {ECO:0000313|EMBL:ACU53047.1, 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 ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP001631; ACU53047.1; -; Genomic_DNA.
DR RefSeq; WP_012784166.1; NC_013124.1.
DR AlphaFoldDB; C7M1J8; -.
DR STRING; 525909.Afer_0076; -.
DR GeneID; 80814264; -.
DR KEGG; afo:Afer_0076; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_11; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000000771; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000000771}.
FT MOD_RES 288
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 458 AA; 50428 MW; 3F78FB5A883A3617 CRC64;
MHRLDDELRS LQASIVRYAM ERIALQPPPL DGPKSADELR ALYGANVTED GIGGEEALRR
FVEGYAPATL SSDHPRFLAF VPVAPTKAAV LFDMIVSASS ISGTSWLEGA GAVYLENEAL
RWLADLIGFP ETAGGTFLSG GSLANLSGLH AARQAAKERL GGVRPDRYRI LASTEAHSSI
RTAADVMDLE VVEVEVNDPG RLRGEDLVRT WAKLTDAERN SVVAVVATAG TTNAGLVDAL
DEVADFAEVN GLWMHVDAAY GGAALASHLR ERFRGIERAG SVVIDPHKWL FAPFDAAAIV
YRDPNVARRA LTQEAAYLDE INRAPDWNPS SYGYHLSRRV RGLPFWFSLA THGTRRYREA
IEASITLAHE SAHEIERRPY LELAIEPELS VVVFRRLGWD AEAYERWSRQ ALVDGVGFVL
PTAYRGEKLL RFCFVNPLTT LDDVRAILDT LAIDPRPW
//