DCUP_BACSU
ID DCUP_BACSU Reviewed; 353 AA.
AC P32395;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Uroporphyrinogen decarboxylase;
DE Short=UPD;
DE Short=URO-D;
DE EC=4.1.1.37;
GN Name=hemE; OrderedLocusNames=BSU10120;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1459957; DOI=10.1128/jb.174.24.8081-8093.1992;
RA Hansson M., Hederstedt L.;
RT "Cloning and characterization of the Bacillus subtilis hemEHY gene cluster,
RT which encodes protoheme IX biosynthetic enzymes.";
RL J. Bacteriol. 174:8081-8093(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=17122346; DOI=10.1128/jb.01083-06;
RA Fan J., Liu Q., Hao Q., Teng M., Niu L.;
RT "Crystal structure of uroporphyrinogen decarboxylase from Bacillus
RT subtilis.";
RL J. Bacteriol. 189:3573-3580(2007).
CC -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC uroporphyrinogen-III to yield coproporphyrinogen-III.
CC {ECO:0000269|PubMed:17122346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 H(+) + uroporphyrinogen III = 4 CO2 + coproporphyrinogen
CC III; Xref=Rhea:RHEA:19865, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57308, ChEBI:CHEBI:57309; EC=4.1.1.37;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17122346}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; M97208; AAA22517.1; -; Genomic_DNA.
DR EMBL; Y14083; CAA74518.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12852.1; -; Genomic_DNA.
DR PIR; B47045; B47045.
DR RefSeq; NP_388893.1; NC_000964.3.
DR RefSeq; WP_009966929.1; NZ_JNCM01000035.1.
DR PDB; 2INF; X-ray; 2.30 A; A/B/C/D=1-353.
DR PDBsum; 2INF; -.
DR AlphaFoldDB; P32395; -.
DR SMR; P32395; -.
DR STRING; 224308.BSU10120; -.
DR jPOST; P32395; -.
DR PaxDb; P32395; -.
DR PRIDE; P32395; -.
DR EnsemblBacteria; CAB12852; CAB12852; BSU_10120.
DR GeneID; 936296; -.
DR KEGG; bsu:BSU10120; -.
DR PATRIC; fig|224308.179.peg.1088; -.
DR eggNOG; COG0407; Bacteria.
DR InParanoid; P32395; -.
DR OMA; LWLMRQA; -.
DR PhylomeDB; P32395; -.
DR BioCyc; BSUB:BSU10120-MON; -.
DR BioCyc; MetaCyc:BSU10120-MON; -.
DR UniPathway; UPA00251; UER00321.
DR EvolutionaryTrace; P32395; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00717; URO-D; 1.
DR Gene3D; 3.20.20.210; -; 1.
DR HAMAP; MF_00218; URO_D; 1.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR Pfam; PF01208; URO-D; 1.
DR SUPFAM; SSF51726; SSF51726; 1.
DR TIGRFAMs; TIGR01464; hemE; 1.
DR PROSITE; PS00906; UROD_1; 1.
DR PROSITE; PS00907; UROD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Lyase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..353
FT /note="Uroporphyrinogen decarboxylase"
FT /id="PRO_0000187584"
FT BINDING 29..33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 78
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:2INF"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 175..198
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 216..222
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 289..293
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2INF"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2INF"
FT HELIX 330..348
FT /evidence="ECO:0007829|PDB:2INF"
SQ SEQUENCE 353 AA; 39647 MW; F499C26BBAFA337E CRC64;
MSKRETFNET FLKAARGEKA DHTPVWYMRQ AGRSQPEYRK LKEKYGLFEI THQPELCAYV
TRLPVEQYGV DAAILYKDIM TPLPSIGVDV EIKNGIGPVI DQPIRSLADI EKLGQIDPEQ
DVPYVLETIK LLVNEQLNVP LIGFSGAPFT LASYMIEGGP SKNYNKTKAF MYSMPDAWNL
LMSKLADMII VYVKAQIEAG AKAIQIFDSW VGALNQADYR TYIKPVMNRI FSELAKENVP
LIMFGVGASH LAGDWHDLPL DVVGLDWRLG IDEARSKGIT KTVQGNLDPS ILLAPWEVIE
QKTKEILDQG MESDGFIFNL GHGVFPDVSP EVLKKLTAFV HEYSQNKKMG QYS
