ID V9TUQ5_9PROT Unreviewed; 393 AA.
AC V9TUQ5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ornithine decarboxylase {ECO:0000256|ARBA:ARBA00034138};
DE EC=4.1.1.17 {ECO:0000256|ARBA:ARBA00034138};
GN Name=ldc {ECO:0000313|EMBL:AHC73882.1};
GN ORFNames=P856_675 {ECO:0000313|EMBL:AHC73882.1};
OS Candidatus Endolissoclinum faulkneri L5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Endolissoclinum.
OX NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73882.1, ECO:0000313|Proteomes:UP000018700};
RN [1] {ECO:0000313|EMBL:AHC73882.1, ECO:0000313|Proteomes:UP000018700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=faulkneri L5 {ECO:0000313|Proteomes:UP000018700};
RX PubMed=24324632;
RA Kwan J.C., Schmidt E.W.;
RT "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT conservation of secondary metabolism.";
RL PLoS ONE 8:E80822-E80822(2013).
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}.
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DR EMBL; CP006745; AHC73882.1; -; Genomic_DNA.
DR RefSeq; WP_025300760.1; NZ_CP006745.1.
DR AlphaFoldDB; V9TUQ5; -.
DR STRING; 1401328.P856_675; -.
DR KEGG; efk:P856_675; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_026444_1_3_5; -.
DR OrthoDB; 9802147at2; -.
DR Proteomes; UP000018700; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
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:UP000018700}.
FT DOMAIN 37..270
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 271..364
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 336
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 393 AA; 43572 MW; B40D01E285339E88 CRC64;
MVDDQDIETD SIRFSDAAAL VTTLKPSYPV YCFRPHKIRA VVQHFIETFP GKVVYAVKCN
IEPRMLSWVS EAGVTAFDTA SLTEIAAVRK QLPDADALFM HPVKSRASIL AADQVYDVST
YCVDSMAELE KVLQVAKRRD LKIFVRVATP RSKATFELSA KFGATQTEAI EILDRVAKER
MQAGIAFHIG SQCINPRAFR TAFAVISDVW RATKAEVREI DVGSGFPVAY AGQSVPPLED
FVKEIVEGRR ETGIDEDVAL LCEPGRALVA DGCSMLCQVY LRKGNKLYLN DGLYGNLSEP
YWARIRLPAR LIRAKNEIHK TNNAPLQDFT IFGPTCDGND FLPTPFRLPH DVREGDWIEV
GQIGAYGAAL STKFNGFFTN VQVELSDEPP PTG
//
