ID L9XWZ4_9EURY Unreviewed; 380 AA.
AC L9XWZ4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Probable porphobilinogen deaminase {ECO:0000256|ARBA:ARBA00021723};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
GN ORFNames=C489_15147 {ECO:0000313|EMBL:ELY65128.1};
OS Natrinema versiforme JCM 10478.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY65128.1, ECO:0000313|Proteomes:UP000011632};
RN [1] {ECO:0000313|EMBL:ELY65128.1, ECO:0000313|Proteomes:UP000011632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY65128.1,
RC ECO:0000313|Proteomes:UP000011632};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
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:ELY65128.1}.
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DR EMBL; AOID01000047; ELY65128.1; -; Genomic_DNA.
DR RefSeq; WP_006432117.1; NZ_AOID01000047.1.
DR AlphaFoldDB; L9XWZ4; -.
DR STRING; 1227496.C489_15147; -.
DR PATRIC; fig|1227496.3.peg.3052; -.
DR OrthoDB; 8042at2157; -.
DR Proteomes; UP000011632; Unassembled WGS sequence.
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; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..160
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 214..264
FT /note="Porphobilinogen deaminase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01379"
FT DOMAIN 280..326
FT /note="Porphobilinogen deaminase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03900"
FT REGION 160..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 380 AA; 41637 MW; B060F541159FBB16 CRC64;
MRTRGTLRLA TRGSALARRQ AALVQEALEE RRYEVELVTV ETTGDQIRDE LIHRLGKTGA
FVRELDERVL EGDLDGAIHS MKDMPTEQPE ELVTAGVPER GRPGDVLITP DGATLSELPD
GATVGTSSLR RRAQLLSERD DLTVEPLRGN VDTRIEKLLA PALQAEHQER TEADKERKGN
TGDEDFEPEY DRTTDEWFDD LSELEKGALG REVETEYDAI VLAQAGLERS GLAHYVEYQE
LPTETFVPAP GQGALAVTAR DDETARDIQT AIDHPRSRVE TTVERTVLAE LGGGCIAPVG
IYAILQGEYV HTTVSVFDRD GEESVTGSRD LPVETHAEAA RQFARDLADR GAADLIAAAR
EDADDDGDEG VSEENKPEGK
//
