ID   A0A143DFX0_9PROT        Unreviewed;       377 AA.
AC   A0A143DFX0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE            EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN   ORFNames=AY555_07290 {ECO:0000313|EMBL:AMW35621.1};
OS   Haematospirillum jordaniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Haematospirillum.
OX   NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW35621.1, ECO:0000313|Proteomes:UP000076066};
RN   [1] {ECO:0000313|EMBL:AMW35621.1, ECO:0000313|Proteomes:UP000076066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5569 {ECO:0000313|EMBL:AMW35621.1,
RC   ECO:0000313|Proteomes:UP000076066};
RA   Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.;
RT   "Complete Genome of H5569, the type strain of the newly described species
RT   Haematospirillium jordaniae.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP014525; AMW35621.1; -; Genomic_DNA.
DR   RefSeq; WP_066136766.1; NZ_JAAVTE010000001.1.
DR   AlphaFoldDB; A0A143DFX0; -.
DR   STRING; 1549855.AY555_07290; -.
DR   GeneID; 53316959; -.
DR   KEGG; hjo:AY555_07290; -.
DR   OrthoDB; 9802241at2; -.
DR   Proteomes; UP000076066; Chromosome.
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; IPR022657; De-COase2_CS.
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.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076066}.
FT   DOMAIN          25..258
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          259..355
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   ACT_SITE        325
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   377 AA;  41227 MW;  15676A9175A58C1F CRC64;
     MTERIHHFLE TRRPEGPCLV VDLDVVRANY QAFATCLPDA RVFYAIKANP APEILSLLAG
     LGSCFDAASV PEIEMALAAG ATPDRISYGN TIKKEADIAR AYQMGITLFA FDAREELEKI
     ARVAPGARVF CRILFDCEGA EWPLSRKFGC EPEMAVELMV YAHALGLRAY GISFHVGSQQ
     SDVGSYDRAL EHVAEIFQAL SEKGIDLSMV NMGGGFPARY LRDIPDVDSY ARAISDALHR
     HFRNRMPETI IEPGRGMVGN AGILQAEVVL ISRKSSRPDE LRWVYLDIGK FGGLAETMGE
     AIRYPIHTPR DGAELAPCVL AGPTCDSADV LYEHTPYPLP VSLEIGDKVL IGSAGAYTTT
     YSAVAFNGFP PLQAFYI
//