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Database: UniProt
Entry: G1Y2N7_9PROT
LinkDB: G1Y2N7_9PROT
Original site: G1Y2N7_9PROT 
ID   G1Y2N7_9PROT            Unreviewed;       376 AA.
AC   G1Y2N7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   Name=speF {ECO:0000313|EMBL:EGY00220.1};
GN   ORFNames=AZA_64673 {ECO:0000313|EMBL:EGY00220.1};
OS   Nitrospirillum amazonense Y2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Nitrospirillum.
OX   NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY00220.1, ECO:0000313|Proteomes:UP000018435};
RN   [1] {ECO:0000313|EMBL:EGY00220.1, ECO:0000313|Proteomes:UP000018435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX   PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA   Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA   Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT   "Genomic insights into the versatility of the plant growth-promoting
RT   bacterium Azospirillum amazonense.";
RL   BMC Genomics 12:409-409(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:326268; EC=4.1.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00034037};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600183-50};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       L-ornithine pathway; putrescine from L-ornithine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00034115}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       {ECO:0000256|ARBA:ARBA00008872, ECO:0000256|RuleBase:RU003737}.
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:EGY00220.1}.
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DR   EMBL; AFBX01000792; EGY00220.1; -; Genomic_DNA.
DR   RefSeq; WP_004273881.1; NZ_AFBX01000792.1.
DR   AlphaFoldDB; G1Y2N7; -.
DR   PATRIC; fig|1003237.3.peg.4177; -.
DR   Proteomes; UP000018435; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR   CDD; cd00622; PLPDE_III_ODC; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR002433; Orn_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR11482; ARGININE/DIAMINOPIMELATE/ORNITHINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR11482:SF6; ORNITHINE DECARBOXYLASE 1-RELATED; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   PRINTS; PR01182; ORNDCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018435}.
FT   DOMAIN          26..258
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          259..354
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        324
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   376 AA;  41195 MW;  18E17D6C70936053 CRC64;
     MTEKIARFFA ENTPATPCLV VDLDVVANNY ANLHDALPEA RIFYAVKANP APEILKLLVE
     RGSCFDTASI PEIQYCLTAG ATADRISFGN TIKKASDIAR AHALGISLFA FDSMEELEKI
     AEHAPGARVF CRILTSGEGA DWPLSRKFGC EPEMATELLL AASTMNVVPY GVSFHVGSQQ
     RDLTQWDKAL AQTAEIFHTL EEKGVMLRMV NLGGGFATRY LKDIPSEGEY GNAIEASLRK
     HFGNRLPETI IEPGRSMVGN AGVIRSEVVL ISRKSHRDER RWVYLDIGKF GGLAETMDEA
     IKYKIQTPHD GGAAEPVILA GPTCDSADVL YEKTEYRLPV DLRIGDKVDI LATGAYTTTY
     SAVNFNGFSP LASYYI
//
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