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Database: UniProt
Entry: A0A238HF93_9NEIS
LinkDB: A0A238HF93_9NEIS
Original site: A0A238HF93_9NEIS 
ID   A0A238HF93_9NEIS        Unreviewed;       355 AA.
AC   A0A238HF93;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|HAMAP-Rule:MF_00218};
DE            Short=UPD {ECO:0000256|HAMAP-Rule:MF_00218};
DE            Short=URO-D {ECO:0000256|HAMAP-Rule:MF_00218};
DE            EC=4.1.1.37 {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|HAMAP-Rule:MF_00218};
GN   Name=hemE {ECO:0000256|HAMAP-Rule:MF_00218,
GN   ECO:0000313|EMBL:SMQ12181.1};
GN   ORFNames=KEBURONENSIS_01115 {ECO:0000313|EMBL:SNB63850.1},
GN   KEBURONENSIS_01191 {ECO:0000313|EMBL:SMQ12181.1};
OS   Kingella negevensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Kingella.
OX   NCBI_TaxID=1522312 {ECO:0000313|EMBL:SMQ12181.1};
RN   [1] {ECO:0000313|EMBL:SMQ12181.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Kingella_eburonensis {ECO:0000313|EMBL:SMQ12181.1};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SNB63850.1, ECO:0000313|Proteomes:UP000215450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kingella_eburonensis {ECO:0000313|EMBL:SNB63850.1};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the decarboxylation of four acetate groups of
CC       uroporphyrinogen-III to yield coproporphyrinogen-III.
CC       {ECO:0000256|HAMAP-Rule:MF_00218}.
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         Evidence={ECO:0000256|HAMAP-Rule:MF_00218,
CC         ECO:0000256|RuleBase:RU000554};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004804, ECO:0000256|HAMAP-Rule:MF_00218,
CC       ECO:0000256|RuleBase:RU000554}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00218}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218}.
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009935, ECO:0000256|HAMAP-Rule:MF_00218,
CC       ECO:0000256|RuleBase:RU004169}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00218}.
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DR   EMBL; FXUV01000016; SMQ12181.1; -; Genomic_DNA.
DR   EMBL; FXUV02000018; SNB63850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238HF93; -.
DR   STRING; 1522312.GCA_900177895_01460; -.
DR   OrthoDB; 9806656at2; -.
DR   UniPathway; UPA00251; UER00321.
DR   Proteomes; UP000215450; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-UniRule.
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   NCBIfam; TIGR01464; hemE; 1.
DR   PANTHER; PTHR21091; METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED; 1.
DR   PANTHER; PTHR21091:SF169; UROPORPHYRINOGEN DECARBOXYLASE; 1.
DR   Pfam; PF01208; URO-D; 1.
DR   SUPFAM; SSF51726; UROD/MetE-like; 1.
DR   PROSITE; PS00906; UROD_1; 1.
DR   PROSITE; PS00907; UROD_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00218};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00218};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00218};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP-
KW   Rule:MF_00218}; Reference proteome {ECO:0000313|Proteomes:UP000215450}.
FT   DOMAIN          22..31
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00906"
FT   DOMAIN          141..157
FT                   /note="Uroporphyrinogen decarboxylase (URO-D)"
FT                   /evidence="ECO:0000259|PROSITE:PS00907"
FT   BINDING         27..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         208
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   BINDING         326
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT   SITE            77
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ   SEQUENCE   355 AA;  39554 MW;  1AA665DFFE0B73B8 CRC64;
     MTQLQNDTFL RALLREPVEY TPIWLMRQAG RYLPEYKATR SFAGNFLDLC HSVDLATEVT
     LQPIDRYNLD AAILFSDILT IPDAMGLGLY FEAGEGPKFE CPLDDEANIE LLTVPDMEKL
     RYVFDAVSSI RKAIDGRVPL IGFSGSPFTL ACYMIEGGGS KDWRKVKTML YSRPDLLHKI
     LDITAQTVTE YLNTQIVCGA QAVQIFDTWG GVLSHSAFQE FSLRYMKQII SGLKRENEGR
     RVPVIVFTKG GGQWLELLAD TGADALGLDW TVEMAQARAR VGDKVALQGN MDPFALFGTQ
     KSICAEVAHI LEAYGNGSGH VFNLGHGINQ FTNPEQVEIL VETVHDLSRH YHQVA
//
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