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Database: UniProt
Entry: A0A0A3ARU7_9PAST
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Original site: A0A0A3ARU7_9PAST 
ID   A0A0A3ARU7_9PAST        Unreviewed;       715 AA.
AC   A0A0A3ARU7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Ornithine decarboxylase {ECO:0000313|EMBL:KGQ70502.1};
GN   ORFNames=OA57_06575 {ECO:0000313|EMBL:KGQ70502.1};
OS   Chelonobacter oris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Chelonobacter.
OX   NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ70502.1, ECO:0000313|Proteomes:UP000030380};
RN   [1] {ECO:0000313|EMBL:KGQ70502.1, ECO:0000313|Proteomes:UP000030380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1662 {ECO:0000313|EMBL:KGQ70502.1,
RC   ECO:0000313|Proteomes:UP000030380};
RA   Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT   "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT   respiratory disease in Hermann's Tortoises.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ70502.1}.
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DR   EMBL; JSUM01000010; KGQ70502.1; -; Genomic_DNA.
DR   RefSeq; WP_034615171.1; NZ_LEKK01000054.1.
DR   AlphaFoldDB; A0A0A3ARU7; -.
DR   STRING; 505317.OA57_06575; -.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000030380; Unassembled WGS sequence.
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   CDD; cd00615; Orn_deC_like; 1.
DR   Gene3D; 3.40.50.220; -; 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; IPR011006; CheY-like_superfamily.
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; IPR027464; Ornithine_deCO2ase_N.
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; SSF52172; CheY-like; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030380}.
FT   DOMAIN          346..360
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         351
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   715 AA;  81142 MW;  D2629FE797AF8FA2 CRC64;
     MKIAASQGTE FAFLSDYKIM DIDMTDFTNV CAVVTTIKDL PEVWEELERL GFAIPIFAAI
     EYGETVPDEW LTELYGVIEL AEDQKYYNGQ LINAAAADYI DTLDPPFFQA LKEYTDYGNA
     AFDCPGHQGG QFFRKHPSGR RFYLYFGETL FRADSCNADV RLGDLLIHEG PAFQAQAHAA
     RVFNADKTYF VLNGTSSANK VAIGALVTKG DLVLFDRNNH KSVHQGALTI SGATPVYMET
     TRNAYGFIGG IPSHCFEEDD IRAQIAKTAP QRANDKRPFR LAVIQLGTYD GTIYNARQVV
     DRIGHLCDYI LFDSAWVGYE QFIPMMRDCS PLLLELNEND PGILVTQSVH KQQAGFSQAS
     QIHKKDNHIR LQARYCNHKR FNNAFMMHAS TSPFYPLFAS LDVNAKMHAG KAGKRMWQEC
     VLSSVEVRKM LLKTCKLIRP FVPPMVDGKS WENHKSEDIA DNIRFFQFAK DARWHDFDGY
     AEEQYFIDPC KLLLTTPGIN METGEYEEFG IPATILAHFL RERSVIPEKA DLNSILFLLT
     PAETMAKFQH LVANIARFEE HIQDNTPVIE MLPTLAKAYP QYGKMRIKEL CQKLHDFYAK
     HRLNELQQYM FLRDAWPKMD ITPDECHNAF IRNQVELVPL SEIRGRTAAE GALPYPPGVL
     CIVPGEIWDG AVLEYFLALE QGINELPGFE PEIQGVYLEA DEFGRKHASA YVLKQ
//
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