ID G1P5I8_MYOLU Unreviewed; 661 AA.
AC G1P5I8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:ENSMLUP00000005279.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005279.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005279.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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:ENSMLUP00000005279.2}
RP IDENTIFICATION.
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; AAPE02011667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006086041.1; XM_006085979.2.
DR AlphaFoldDB; G1P5I8; -.
DR STRING; 59463.ENSMLUP00000005279; -.
DR Ensembl; ENSMLUT00000005777.2; ENSMLUP00000005279.2; ENSMLUG00000005768.2.
DR GeneID; 102426149; -.
DR KEGG; mlf:102426149; -.
DR CTD; 3067; -.
DR eggNOG; KOG0628; Eukaryota.
DR GeneTree; ENSGT00940000157938; -.
DR HOGENOM; CLU_011856_3_0_1; -.
DR InParanoid; G1P5I8; -.
DR OMA; MKREDSC; -.
DR OrthoDB; 47798at2759; -.
DR TreeFam; TF313863; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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:UP000001074}.
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 661 AA; 73387 MW; CA7A295A88E92D60 CRC64;
MMEPEEYRER GKEMVDYICQ YLSSVRERRV TPDVRPGYLR AQLPESAPED PDSWDSIFGD
IERVIMPGVV HWQSPHMHAY YPALTSWPSL LGDMLADAIN CLGFTWASSP ACTELEMNVM
DWLAKMLGLP EHFLHHHPGS HGGGVLQSTV SESTLIALLA ARKNKILEMK ASEPGADESS
LNARLIAYAS DQAHSSVEKA GLISLVKMKF LPVDSNFSLR GEALQKAIEE DKERGLVPVF
VCATLGTTGV CAFDCLSELG PICAREGLWL HIDAAYAGTA FLCPEFRGFL QGIEYADSFT
FNPSKWMMVH FDCTGFWVKN KYKLQQTFSV NPVYLRHANS GAATDFMHWQ IPLSRRFRSI
KLWFVIRSFG VKNLQAHVRH GTEMAKYFES LVRKDPFFEI PAKRHLGLVV FRLKGPNCLT
ESVLKEIAKA GQIFLIPATV QDKLIIRFTV TSQFTTRDDI LRDWNLIRDA ATLILSQHCT
SQPSPQARGL IPQARGPRAL SSGGALQSVG GAEDDLAQAR RIAKQPQPVG AGLGREDACP
LDTLLDPLDD CFSEEAPAEA KRKLSSFLIN YLSVRNKRKA VRSLSCNSVP VSAQKPLSSE
GPVKNGGSST VNILSRFPEE VMMLKKSAFK KLIKFYSVPS FPECSLQCGL QLPCCPLQAT
V
//
