ID A0A2P7YCP9_9ASCO Unreviewed; 955 AA.
AC A0A2P7YCP9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Uroporphyrinogen decarboxylase {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|RuleBase:RU000554};
DE EC=4.1.1.37 {ECO:0000256|ARBA:ARBA00012288, ECO:0000256|RuleBase:RU000554};
GN ORFNames=C7M61_005206 {ECO:0000313|EMBL:PSK33740.1};
OS [Candida] pseudohaemulonii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK33740.1, ECO:0000313|Proteomes:UP000241107};
RN [1] {ECO:0000313|EMBL:PSK33740.1, ECO:0000313|Proteomes:UP000241107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B12108 {ECO:0000313|EMBL:PSK33740.1,
RC ECO:0000313|Proteomes:UP000241107};
RA Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA Cuomo C.A.;
RT "Candida pseudohaemulonii genome assembly and annotation.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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|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|RuleBase:RU000554}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009935, ECO:0000256|RuleBase:RU004169}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSK33740.1}.
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DR EMBL; PYFQ01000023; PSK33740.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7YCP9; -.
DR STRING; 418784.A0A2P7YCP9; -.
DR EnsemblFungi; C7M61_005206_t1; PSK33740.1; C7M61_005206.
DR VEuPathDB; FungiDB:C7M61_005206; -.
DR OrthoDB; 34606at2759; -.
DR UniPathway; UPA00251; UER00321.
DR Proteomes; UP000241107; Unassembled WGS sequence.
DR GO; GO:0004853; F:uroporphyrinogen decarboxylase activity; IEA:UniProtKB-EC.
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 Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR HAMAP; MF_00218; URO_D; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR038071; UROD/MetE-like_sf.
DR InterPro; IPR006361; Uroporphyrinogen_deCO2ase_HemE.
DR InterPro; IPR000257; Uroporphyrinogen_deCOase.
DR InterPro; IPR041175; VLRF1/Vms1.
DR NCBIfam; TIGR01464; hemE; 1.
DR PANTHER; PTHR21091; METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED; 1.
DR PANTHER; PTHR21091:SF169; UROPORPHYRINOGEN DECARBOXYLASE; 1.
DR Pfam; PF18826; bVLRF1; 1.
DR Pfam; PF01208; URO-D; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 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 Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW ECO:0000256|RuleBase:RU000554};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000554};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000554};
KW Reference proteome {ECO:0000313|Proteomes:UP000241107}.
FT DOMAIN 25..34
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00906"
FT DOMAIN 147..163
FT /note="Uroporphyrinogen decarboxylase (URO-D)"
FT /evidence="ECO:0000259|PROSITE:PS00907"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 107522 MW; 7081E1B066D27EE4 CRC64;
MPSFEPLKND LILRAAKGEK VERPPIWIMR QAGRYLPEYH EVKGGRDFFE TCRDAEIASE
ITIQPVDHFD GLIDAAIIFS DILVIPQAMG FEINMIEGKG PVFADPLRSR EDINRINLKP
DVLKSLDWAY KAITLTRTKL KGRVPLLGFC GAPWTLLVYM TEGQGSKMFR FAKQWIYEYT
KESHTLLQAT TDACIEFLAQ QVVAGAQMLQ VFESWAGELG PHEFDEFCLP YLRQIAAKLP
GRLAELGVKE KIPLTVFAKG AWYALDELCE SGYDTVSLDW LYKPEDAVKV VNGRRITLQG
NLDPGIIYGS DEVISKKVEQ MIKGFGGGKQ NYIVNFGHGT HPFMKPEKIE HFLKECHRFG
SYYYFFTARM TSVAKDDLYI FSLDEAVKNS LSLLHFDESA AVVAVNEAPV ETKSPIENQI
VDPKTEPEKS KDYYKSDLHR LNLKRQVNSL PPLTEDEFDK LIETQSVESI SGSEESETED
EEDNKLNTIF EQLSTKNEDE EQSVSHMNTN SPYILFQSSL VDQGKAFGLY KALFSKASLD
TGNVLEEVSQ ISSEPKRLGT SVLLMIGGGH FAGAVVSHTP KNIKGLAPNH KIPKQEQQVN
VLQSKTFHRY TTRRKQGGSQ SASDNSRGKA NSAGSSIRRY NEQALQQEVR ELLNLWKSYL
QNADFVFIRA NAVANRRALV GYEGAPLAAD DKRIRNFPFT TKRATLSELK RAWVQLAHMQ
VVDLPKAKKV TEKKTDISKV QKTPSPAPEL SESDKHTKEI INLLKKLKAP MLINYLKKNG
LDANYQFTPG NQHAHAPTPL HYAASQGLHH MIQVLLVNLK ADPTILNAIG KTAAQMSSTS
TAKKTFQIAR NTLGEEFTDW NAAKVGPPRT REEVAKEEEQ QKKQQEAENR RLIEEELAKK
TEMEQKKPTF SSGGTLGGKV QNRPSETSEL TEQQKTRLMR EQRARAAEAR MKMLL
//
