ID A0A1F2P6R1_9EURY Unreviewed; 1353 AA.
AC A0A1F2P6R1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE SubName: Full=Alpha-D-phosphohexomutase, alpha/beta/alpha domain protein I domain protein {ECO:0000313|EMBL:OFV67017.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:OFV67017.1};
GN ORFNames=SBU_000310 {ECO:0000313|EMBL:OFV67017.1};
OS Candidatus Syntropharchaeum butanivorans.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanosarcinales; ANME-2 cluster;
OC Candidatus Syntropharchaeum.
OX NCBI_TaxID=1839936 {ECO:0000313|EMBL:OFV67017.1, ECO:0000313|Proteomes:UP000185779};
RN [1] {ECO:0000313|EMBL:OFV67017.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BOX1 {ECO:0000313|EMBL:OFV67017.1};
RA Laso-Perez R., Richter M., Wegener G., Musat F.;
RT "Microbial consortia oxidize butane by reversing methanogenesis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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:OFV67017.1}.
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DR EMBL; LYOR01000001; OFV67017.1; -; Genomic_DNA.
DR STRING; 1839936.SBU_000310; -.
DR PATRIC; fig|1839936.3.peg.313; -.
DR Proteomes; UP000185779; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd07010; cupin_PMI_type_I_N_bac; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR049071; MPI_cupin_dom.
DR InterPro; IPR046457; PMI_typeI_cat.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF2; PHOSPHOMANNOMUTASE_PHOSPHOGLUCOMUTASE; 1.
DR Pfam; PF21621; MPI_cupin_dom; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR Pfam; PF20511; PMI_typeI_cat; 1.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OFV67017.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000185779}.
FT DOMAIN 510..587
FT /note="Phosphomannose isomerase type I catalytic"
FT /evidence="ECO:0000259|Pfam:PF20511"
FT DOMAIN 723..776
FT /note="Mannose-6-phosphate isomerase cupin"
FT /evidence="ECO:0000259|Pfam:PF21621"
FT DOMAIN 787..900
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 1014..1103
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 1107..1222
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 1241..1323
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 1353 AA; 154021 MW; 940EE69921B47E17 CRC64;
MSTCYYTHIQ RMDEIIQGSE GFDLVIIVTS SDKQAAFWKE RLEAVKDQII GKDARIYCVV
EEWEAGQLLG TLNAWEKVSA YEDLESLLRQ GGKIAIYHTA GYGKRMAPLV QSEGNDKAGI
KLPGLLNLSG RKVPMRLLEA VIYQSSIFAP SRKGRICVFW ADQIFIPSGD VEFEGKHHVE
LFTIRKPAPD TREEWEREWQ AYGLVIPRED GCMMLEKQSW DEFERLVEDG VIKQEDGRII
IGKGLGCFSI SYEFFIEVLS EFKKDLEERR KLDTDPDLWM PLTSPDRVEP EKRARVEPLI
KRFDSKGAIF GDKDMGAGTY WWDLGQPILY HEHLLKLTQD TEEGEVMRAF FRADSSGIIG
SEVEGMLRGC VVVDSRVEDS DLNECVVISS MIRGVSGNKS LIYNCIELSG FDLGDENVVA
DLFHPMKGKI RMKRGILRDG KKDWDMRLLP NPYSYRELEH LMRDVPIDDT LRERETWERY
WRLNLGDKFE QLSRSVIRLS GSTLEKPWGS ESWICSGHPK NPSMIKVGEI DVSLIHLLNH
RGEEIIGDQL YRDFRGEFPV ILKFIYAREN LSVQVHPSDD DAARLGEPEP GKTEGWYVID
AEPGAKIYLS LRRQIADLSE ICEDVLHGVE IKKGDVFLVP PGTLHAIGAG THLFEIQESS
DLTYRVWDWG RQRETHLDKA CLVSITDQDA ESLKQTPREI DGETVLLDTV YFTLSLASSG
LQETKGSFHT LTCIEGEAEI EYNGRKERLS TGETALIPAS ITSYMLRSNG KVLKSYLRTP
SHIDPVIFQT YDVRAPETML PDRICYYLGK GYGTYLRRER GEESEHWVCV GGGIRLSTER
IRKALIDGIR SSGVNVYDIG ITSTPELYFA IPFLHADGGI NITASHNEAI YNGLKQVIRS
DDEFIMSINA DQMLEIKRII LGSDFLYGKG ERVKVKDGLI PRYHNLLVES NCRLGREIWI
HLLREWDLKE LLDTLAEIEF PGKADGKRWQ EIKKRLRIPD EIEMPETAVA APLDGLKVVI
DFGNGSTWRT KSVYLNLGCE VVGLNETPDG RFPAHHPDPI KAKYRRQLEE LTVKVAESEK
EKEVVGFGHD EDGDRVIFVR SDGRVVEGDR TLAIQAKDII EEYRKKGKVP RFMGEVKFSR
VTEEFITSHG GIYIMSPTGF AFIKERMKEI YLASKEKGEE GVVLAAELSG HQMSGQEENW
MFDDGTLAAV KILSVIAKAK RRGRTFIDLD EEVPRYPATP EINIRLPTNH LDEKEEVVRK
ALEIFEAMGF EIDRTDGGII RWYDDKGWVG QALIRKSNTQ PMVICRVEGR DEAAKARVEE
EFFGVLKKVS TERIPRLDLG SDDYVREWMS RGT
//
