ID A0A1H6MKR7_9FLAO Unreviewed; 344 AA.
AC A0A1H6MKR7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=SAMN02927937_02650 {ECO:0000313|EMBL:SEI00027.1};
OS Paenimyroides aquimaris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=1159016 {ECO:0000313|EMBL:SEI00027.1, ECO:0000313|Proteomes:UP000199634};
RN [1] {ECO:0000313|EMBL:SEI00027.1, ECO:0000313|Proteomes:UP000199634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10825 {ECO:0000313|EMBL:SEI00027.1,
RC ECO:0000313|Proteomes:UP000199634};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNXE01000053; SEI00027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6MKR7; -.
DR STRING; 1159016.SAMN02927937_02650; -.
DR OrthoDB; 9806656at2; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000199634; 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:UP000199634}.
FT DOMAIN 20..29
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00906"
FT DOMAIN 139..155
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00907"
FT BINDING 25..29
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
FT SITE 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00218"
SQ SEQUENCE 344 AA; 38604 MW; 7A5FA42854DD99BE CRC64;
MLKNDLFLRA LKGETIERPP VWMMRQAGRY LPEFRALRDK YDFFTRCRMP EIAAEITVQP
IRIVKPDAAI LFSDILVVPQ AMNIEVEMKE NVGPWLPNPI RSAADVEEVI VPNIEETLGY
VMDAVKVTKE MLNDEVPLIG FAGSPWTIFC YAVEGKGSKS FDKAKGFCFS QPEAAHALLQ
KITDTTILYL KEKVKAGVNA VQIFDSWGGM LSPVDYQEFS WKYINQIVEA LADETEVIVF
GKGCWFALGD MARSKASALG VDWTCSARNA RYLSGGNITL QGNFDPSRLL SPIPTIKKMV
HEMIDEFGKD KYIVNLGHGI LPNIPVDHAK AFVEAVKEYN PARF
//
