ID H0WB71_CAVPO Unreviewed; 642 AA.
AC H0WB71;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Histidine decarboxylase {ECO:0000256|ARBA:ARBA00039946};
DE EC=4.1.1.22 {ECO:0000256|ARBA:ARBA00012320};
GN Name=HDC {ECO:0000313|Ensembl:ENSCPOP00000020237.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000020237.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000020237.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000020237.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533}.
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DR EMBL; AAKN02027786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0WB71; -.
DR STRING; 10141.ENSCPOP00000020237; -.
DR Ensembl; ENSCPOT00000019608.2; ENSCPOP00000020237.2; ENSCPOG00000027120.2.
DR VEuPathDB; HostDB:ENSCPOG00000027120; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000157938; -.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; H0WB71; -.
DR OMA; MKREDSC; -.
DR TreeFam; TF313863; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000027120; Expressed in hypothalamus and 5 other cell types or tissues.
DR GO; GO:0004398; F:histidine decarboxylase activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0001694; P:histamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0006548; P:histidine catabolic process; IEA:Ensembl.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR PANTHER; PTHR11999:SF68; HISTIDINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 3: Inferred from homology;
KW Catecholamine biosynthesis {ECO:0000256|ARBA:ARBA00022584};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT MOD_RES 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 642 AA; 71862 MW; 39240695EE5EEEA3 CRC64;
MVDYICQYLS TVRDRRVTPD VQPGYLRAQL PESAPEEPDS WDSIFGDIER IIMPGVVHWQ
SPHMHAYYPA LTSWPSLLGD MLADAINCLG FTWASSPACT ELEMNMMDWL AKMLGLPDHF
LHGHPSSQGG GVLQSTVSES TLIALLAARK NKILEMQKSE PEVDDSSLNA RLVAYASDQA
HSSVEKAGLI SLVKMRFLPV DDNFSLRGEA LQKAIQEDRR RGLVPVFVCA TLGTTGVCAF
DCLSELGPIC AKEGLWLHID AAYAGTAFLC PEFRDFLKGI DFADSFTFNP SKWMMVHFDC
TGFWVKDKVK LQQTFSVNPV YLRHANSGTA TDFMHWQIPL SRRFRSIKLW FVIRSFGVKN
LQAHVRHGIE MAKIFESLVR NDPFFEIPAK RHLGLVVFRL KGPNCLTESV LKEIAKDGRL
FLIPATIQNK LIIRFTVTSQ FTTRDDILRD WNLIRDAATL VLSQHCTSQP SPQTRGYRTL
AGGMPLPPVH GGGDDPAQAR KIIKQPQRMG TIPVRREDGC HLETLADPLD DCFSEEAPDV
SKHKLSSFLF SYLSVQHKKK TVRSLSCNSV PVSAQKLFPA EGSAKNGGTS RVRLFSRFPE
EMMILKKSAF KKLIKFYSVP SFPECSSQCG LQLPCCPLQA MV
//
