ID D1P605_9GAMM Unreviewed; 822 AA.
AC D1P605;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Orn/Lys/Arg decarboxylase, major domain protein {ECO:0000313|EMBL:EFB71128.1};
GN ORFNames=PROVRUST_07669 {ECO:0000313|EMBL:EFB71128.1};
OS Providencia rustigianii DSM 4541.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB71128.1, ECO:0000313|Proteomes:UP000005512};
RN [1] {ECO:0000313|EMBL:EFB71128.1, ECO:0000313|Proteomes:UP000005512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB71128.1,
RC ECO:0000313|Proteomes:UP000005512};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:EFB71128.1}.
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DR EMBL; ABXV02000042; EFB71128.1; -; Genomic_DNA.
DR AlphaFoldDB; D1P605; -.
DR STRING; 500637.PROVRUST_07669; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_014292_3_0_6; -.
DR Proteomes; UP000005512; 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; 3.40.50.2300; -; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1}.
FT DOMAIN 55..169
FT /note="Orn/Lys/Arg decarboxylase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03709"
FT DOMAIN 175..629
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 655..783
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
FT MOD_RES 420
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 822 AA; 92920 MW; 9948BC70841BCABC CRC64;
MIYFPTSFIK EWVSIYDCQF FAVNNKIKWR YILKFNHNIL FVSSSYLKED HPAKQALERL
KAAVIERDFK VFIADKIQDG IRLIQENPKY SAVAIYWDDN DPNMAKNCVQ VVAVLRKRNP
TTPLLLVSEE NITDNVPLDV LKEVSEYIYL YSETPPFTAN RIYTLVHRYA ENLLPPYFKT
LKDFTEDGDY YWDCPGHMGG MAYLKHPVGI EFINFFGENM MRADIGVATA EMGDYLIHAG
PSKKSEEIAA ELFGADWTFY GVSGSSGSNR IVAQGAVAAD EIVIVDRNCH KSLNHGLTLS
QARPVYLKPT RNGYGLIGPI PNERLKKASI DKLIAQSPLS QGAATSEATY AVVTNCTYDG
FCYNVNDVVK YLGESAPRIH FDEAWYAYAR FHPLYKNRFA MGVEDTPNRP TIFAVQSTHK
MLPSLSMASM IHVKKSERAP LNFDDFNDSF MMHGTTSPYY PIIASIDVAV SMMQGQSGTS
LVQESIEEAI AFRKAVVSVK RQLKEQEGES AWFFDVLQPT EVKNQETGQK YSFEDAPIEL
LSQDPNCWGL RAGDKWHGFT DEDLADTNSM LDPVKVTITC PGISPDGKYQ DRGIPGYIIT
KFLDDRRIEI ARTGDYTILI LFSVGITKGK WGTLLESLLS FKKLYDNGTL AIDAIPSLKN
HSSNYDKLTL KQLCQEMHEK MCDLDLMKHI NDAVNTDPEP VLTPADAYQK VVRYKSEHIR
LDDFSGRIAA SMLVPYPPGI PVLMPGERLP KGNQGIIGYL RALQEFDKHY PGFEHEVQGI
NVDDNGDFWV RAIIEDDRKA VEVPKHITFK RHVTSTIKKG RQ
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