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Database: UniProt
Entry: A1KAF9_AZOSB
LinkDB: A1KAF9_AZOSB
Original site: A1KAF9_AZOSB 
ID   A1KAF9_AZOSB            Unreviewed;       747 AA.
AC   A1KAF9;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Orn/arg/lys decarboxylase {ECO:0000313|EMBL:CAL95815.1};
DE            EC=4.1.1.- {ECO:0000313|EMBL:CAL95815.1};
GN   Name=adiA {ECO:0000313|EMBL:CAL95815.1};
GN   OrderedLocusNames=azo3199 {ECO:0000313|EMBL:CAL95815.1};
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL95815.1, ECO:0000313|Proteomes:UP000002588};
RN   [1] {ECO:0000313|EMBL:CAL95815.1, ECO:0000313|Proteomes:UP000002588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72 {ECO:0000313|EMBL:CAL95815.1,
RC   ECO:0000313|Proteomes:UP000002588};
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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DR   EMBL; AM406670; CAL95815.1; -; Genomic_DNA.
DR   RefSeq; WP_011766923.1; NC_008702.1.
DR   AlphaFoldDB; A1KAF9; -.
DR   STRING; 62928.azo3199; -.
DR   KEGG; azo:azo3199; -.
DR   eggNOG; COG1982; Bacteria.
DR   HOGENOM; CLU_014292_3_0_4; -.
DR   Proteomes; UP000002588; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005308; OKR_de-COase_N.
DR   InterPro; IPR011193; Orn/lys/arg_de-COase.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   Pfam; PF03709; OKR_DC_1_N; 1.
DR   PIRSF; PIRSF009393; Orn_decarb; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CAL95815.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002588}.
FT   DOMAIN          390..404
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         395
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   747 AA;  84365 MW;  FF5DD07A0A4DC642 CRC64;
     MRFHFPIIII DEDFRSENTS GLGIRALATA IEEEGMEVLG VTSYGDLTSF AQQQSRGSGF
     ILSIDDEEFS SPEASAKAIA DLRSFVEEIR LRNADIPIFL HGETRTSRHI PNDVLREMHG
     FIHMFEDTPE FIARYVVREA RNYLESLPPP FFRALTHYAA DGSYSWHCPG HSGGVAFLKS
     PVGQMFHQFF GENMLRADVC NAVDELGQLL DHTGPVAASE RNAARIFNCD HLYFVTNGTS
     TSNKMVWHTT VAPGDIVVVD RNCHKSILHS IIMTGAVPVF LTPTRNHYGI IGPIPLEEFS
     MENIQKKIEA NPFAREAKSK KPRILTITQS TYDGVVYNVE TIKEMLDGKI DTLHFDEAWL
     PHAAFHDFYG DYHAIGEDRP RCRESMIFST QSTHKLLAGL SQASQILVQD SQTRKLDRDI
     FNEAYLMHTS TSPQYAIIAS CDVAAAMMEP PGGAALVDES LAEAVEFRRA MRKVDAEFGE
     SDWWFRVWGP EYLAEEGLGE RDDWMLKNGE RWHGFGDLAP GFNMLDPIKA TVITPGLDVD
     GDFADWGIPA GILTRYLAEH GIIVEKTGLY SFFIMFTIGI TKGRWNTLVT ELQQFKDDYD
     RNQPLWRVMP DFIAKHPRYE KVGLKDLCAQ IHSFYKAHDV ARLTTEMYLS DMVPAMKPAD
     AFAKMAHREI ERVLIDELED RVTAMLVTPY PPGIPLLIPG ERFNPTIVRY LQFARDFNAR
     FPGFETDIHG LVKGDDGRYY VDCVAAD
//
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