ID A0A0F7KCH4_9PROT Unreviewed; 440 AA.
AC A0A0F7KCH4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Histidine decarboxylase {ECO:0000313|EMBL:AKH36833.1};
GN ORFNames=AAW31_01860 {ECO:0000313|EMBL:AKH36833.1}, BCL69_10685
GN {ECO:0000313|EMBL:TYP78776.1};
OS Nitrosomonas communis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=44574 {ECO:0000313|EMBL:AKH36833.1, ECO:0000313|Proteomes:UP000034156};
RN [1] {ECO:0000313|Proteomes:UP000034156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|Proteomes:UP000034156};
RA Kozlowski J.A., Kits K.D., Stein L.Y.;
RT "Draft genome of Nitrosomonas communis strain Nm2.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKH36833.1, ECO:0000313|Proteomes:UP000034156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|EMBL:AKH36833.1,
RC ECO:0000313|Proteomes:UP000034156};
RX PubMed=26769932;
RA Kozlowski J.A., Kits K.D., Stein L.Y.;
RT "Genome Sequence of Nitrosomonas communis Strain Nm2, a Mesophilic Ammonia-
RT Oxidizing Bacterium Isolated from Mediterranean Soil.";
RL Genome Announc. 4:0-0(2016).
RN [3] {ECO:0000313|EMBL:TYP78776.1, ECO:0000313|Proteomes:UP000324176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm2 {ECO:0000313|EMBL:TYP78776.1,
RC ECO:0000313|Proteomes:UP000324176};
RA Wagner M.;
RT "Active sludge and wastewater microbial communities from Klosterneuburg,
RT Austria.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP011451; AKH36833.1; -; Genomic_DNA.
DR EMBL; VNHT01000068; TYP78776.1; -; Genomic_DNA.
DR RefSeq; WP_046848935.1; NZ_VNHT01000068.1.
DR AlphaFoldDB; A0A0F7KCH4; -.
DR KEGG; nco:AAW31_01860; -.
DR PATRIC; fig|44574.3.peg.440; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000034156; Chromosome.
DR Proteomes; UP000324176; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF18; HISTIDINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000034156}.
FT MOD_RES 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 440 AA; 49372 MW; 31D83D8AC8B1099B CRC64;
MLMNRRQSLG LSGPTALMAT CYPNITPGHA LLSHPQQPSA ELLKSMKELP KQKNMLLGYP
LNMATPPEEF FVWRKELFSA GLNQFGFNNV GNPYAHSHIP FNSHLFEREL INRFGTVYGF
SQDNVWGFLS NSGTDSNMHG LYMGRTLLRS QTGVMPKIYF TREAHYSIQI LTDLLNLEWV
VVGTDRDGSM DIDDLERQLK ANANYPALVV ATIGTTFKGA VDSIDGIQAK LKGRTAYLHL
DAALFGGYLP HTQFAAELLH EISDEGTGRK VKRYDSIAVS CHKFFGFPAP AGLFITTRAN
FEMFLTQFGQ IHDPEYILQI PGTITCSRDA MKAAEFYFFS SEAAFSKQAA DAKSMLDNTT
YLLKEMMAHY DYLQPVRANP QSNTIYFRKP GDTVVNRYSL AAMGVEIDKE HVPHVHVVVM
PHASKEILDQ FLTDLGKKEE
//
