ID A0A0N7L9N5_9BASI Unreviewed; 698 AA.
AC A0A0N7L9N5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Porphobilinogen deaminase {ECO:0000256|ARBA:ARBA00016519};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00033064};
DE AltName: Full=Pre-uroporphyrinogen synthase {ECO:0000256|ARBA:ARBA00030685};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH14282.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH14282.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000256|ARBA:ARBA00001916};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004735}.
CC -!- SIMILARITY: Belongs to the HMBS family.
CC {ECO:0000256|ARBA:ARBA00005638}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCYA01000240; CEH14282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N7L9N5; -.
DR STRING; 401625.A0A0N7L9N5; -.
DR OrthoDB; 788at2759; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000054845; Unassembled WGS sequence.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR Gene3D; 3.30.160.40; Porphobilinogen deaminase, C-terminal domain; 1.
DR InterPro; IPR000860; HemC.
DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR InterPro; IPR022417; Porphobilin_deaminase_N.
DR InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR NCBIfam; TIGR00212; hemC; 1.
DR PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF03900; Porphobil_deamC; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 2.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE 3: Inferred from homology;
KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 192..372
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 402..428
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 74027 MW; 9363225B1B4D3CCB CRC64;
MASSTVYVER HPDEGTAQCP VAHDPAQPLP PGHPPTSSHP ASSLKPPTAP GCIFFRTTDD
LIVTPPLSRV GSAKLDDLKA TANINPLAPG AGQSLDPDTS LVLASRNSQL ALVQSSHVSA
MLSSHYSHRS PAFVSFTREQ ATLAGQSSSA KAGSTITPPS TPPSLPSLPT FDAETISTAQ
SRIAALGIPG PCSFPITSMS TAGDHNQRSP LYVIGGDGKA IWTKELEVAL SGGAVDAIVH
CLKDVPTALP DGLMLGAILE REDPRDALVV KRGLPYKTLD ELPPGSVIGT SSVRRVAQLR
RRYPELVFSD VRGNLNTRLS KLDAPNGPYT ALVLAAAGLI RLNLTARITA FLSAPVLMYS
VGQGALAIEV RTPPPGADPR TNREARILEM IRSISDWRAT WRAEAERALL RELEGGCSIP
VGVETRFADH AAVEGQRNEG EALRLVAASR GVDVEDTREE EGHTIPPDEI TSTSGAPTRP
AALERLNTDK IDVATAQAAS TSATPAPTPV IKAAEEYYPE DRAAAPAEGA ELTLHAIVVS
LDGKRSCDYT LTRHCMDVAD AQALGRAVAQ ELAQSRGARA ILEEVERHRK LAEAADERRR
REGRAQRVAE VAGKAEAAAH EGDVLEGIGE EKQSSDAIDE AEARRKLQEV LEAAKNGNGD
RTRSGSLLNG DVPHGLLANE TDRRGIPRSD GLPKAWEV
//
