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Database: UniProt
Entry: L0IHD2_HALRX
LinkDB: L0IHD2_HALRX
Original site: L0IHD2_HALRX 
ID   L0IHD2_HALRX            Unreviewed;       378 AA.
AC   L0IHD2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Probable porphobilinogen deaminase {ECO:0000256|ARBA:ARBA00021723};
DE            EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN   OrderedLocusNames=Halru_3085 {ECO:0000313|EMBL:AGB17651.1};
OS   Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halovivax.
OX   NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB17651.1, ECO:0000313|Proteomes:UP000010846};
RN   [1] {ECO:0000313|Proteomes:UP000010846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18193 / JCM 13892 / XH-70
RC   {ECO:0000313|Proteomes:UP000010846};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Halovivax ruber XH-70.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC         Evidence={ECO:0000256|ARBA:ARBA00001916};
CC   -!- SIMILARITY: Belongs to the HMBS family.
CC       {ECO:0000256|ARBA:ARBA00005638}.
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DR   EMBL; CP003050; AGB17651.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0IHD2; -.
DR   STRING; 797302.Halru_3085; -.
DR   KEGG; hru:Halru_3085; -.
DR   eggNOG; arCOG04299; Archaea.
DR   HOGENOM; CLU_019704_1_0_2; -.
DR   OrthoDB; 8042at2157; -.
DR   Proteomes; UP000010846; Chromosome.
DR   GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4.
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; 2.
DR   Pfam; PF03900; Porphobil_deamC; 1.
DR   PRINTS; PR00151; PORPHBDMNASE.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 2.
DR   SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
DR   PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
PE   3: Inferred from homology;
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..162
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          214..263
FT                   /note="Porphobilinogen deaminase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01379"
FT   DOMAIN          280..335
FT                   /note="Porphobilinogen deaminase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03900"
FT   REGION          162..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  41262 MW;  2005BE4041BC9B4D CRC64;
     MKSRGTLRLA TRGSLLARRQ AGMVGERLEE RRYDVDLVTV ETTGDQLADE LIHRLGKTGA
     FVRELDERVL DGDCDAAIHS LKDVPTEQPD ELVTAAVPER GPAEDVLLTP EGTTLDDLPR
     GATVGTSSLR RRALLLDQRP DLTVEPLRGN VDTRIEKLLA PTLQAEHEAR TEADKERKGH
     AGDEDFEPEY DRTVEEWFDD RSELEKGALG REVETEYDAI VLARAGLERS GLAHAVDFEP
     LSLTTFVPSP GQGALCVTAT DGETAREIQS AIDHPRSRVE VTVERTILAT LGGGCIAPLG
     IHAVVQGEYV HTAVAVYDRD GETSVKATRD LPIETHATAA REFADELADR GAAELIEESR
     KELEDDGEPA PEDQPEGK
//
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