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Database: UniProt
Entry: F7CVL5_MONDO
LinkDB: F7CVL5_MONDO
Original site: F7CVL5_MONDO 
ID   F7CVL5_MONDO            Unreviewed;       667 AA.
AC   F7CVL5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 2.
DT   27-MAR-2024, entry version 66.
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:ENSMODP00000002787.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000002787.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000002787.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000002787.3}
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   RefSeq; XP_001380521.1; XM_001380484.3.
DR   AlphaFoldDB; F7CVL5; -.
DR   STRING; 13616.ENSMODP00000002787; -.
DR   Ensembl; ENSMODT00000002842.4; ENSMODP00000002787.3; ENSMODG00000002284.4.
DR   GeneID; 100031203; -.
DR   KEGG; mdo:100031203; -.
DR   CTD; 3067; -.
DR   eggNOG; KOG0628; Eukaryota.
DR   GeneTree; ENSGT00940000157938; -.
DR   HOGENOM; CLU_011856_3_0_1; -.
DR   InParanoid; F7CVL5; -.
DR   OMA; MKREDSC; -.
DR   OrthoDB; 47798at2759; -.
DR   TreeFam; TF313863; -.
DR   Proteomes; UP000002280; Chromosome 1.
DR   Bgee; ENSMODG00000002284; Expressed in blood and 10 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004398; F:histidine decarboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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:UP000002280}.
FT   REGION          584..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   667 AA;  74781 MW;  EB3648E8AC1D8F32 CRC64;
     MDLEEYRERG KEMVDYIFQY LSTVRERRVT PDVQPGYMRS QLPDSAPVEP DSWDTIFGDI
     EKIIMPGVVH WQSPHMHAYF PALTSWPSLL GDMLADAINC LGFTWASSPA CTELEMNVMD
     WLAKMLGLPE HFLHHHPGSQ GGGVLQSTVS ESTLVALLAA RKNKILNMKV SEPDVDESSL
     NSRLIAYASD QAHSSVEKAG LISLVKMKFL PVDKNFSLRG ETLQKAIEED KKQGLVPVFV
     CATLGTTGVC AFDCLAELGP ICASEGLWLH VDAAYAGTAF LCPEFREFLK GIEYADSFTF
     NPSKWMMVHF DCTGFWVKDK FKLQQTFSVN PVYLRHANSG AATDFMHWQI PLSRRFRSIK
     LWFVIRSFGV KNLQAHVRHG TEMAKYFESL VRNDPLFEIP AKRHLGLVVF RLKGPNCLTE
     KVLKELVKSG YLFLIPAIIQ DKFIIRFTVT SQFTTKEDIL RDWNLIRDAA THILSQHCTS
     QPTPQDGNTI PRANGLRGMA SGMPLQAQGN AGEDLEGPRK IVAQPQHMEV RPMRREVSQP
     LENQLDPLDD CFSEEGPEIT KHKLSSFLFS YLSVQNKKKT VRSLSCNSVP TGGPRDLLGQ
     KQGPAEAPGK SGGSARSKIL SRFPEEMMML KKSAFKRLIK FYSVPSFPEC SIQCGIQLPC
     CPLQAIV
//
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